SARS-CoV-2 Omicron variant shows less efficient replication and fusion activity when compared with Delta variant in TMPRSS2-expressed cells
Open accessAbstract
The novel SARS-CoV-2 Omicron variant (B.1.1.529), first found in early November 2021, has sparked considerable global concern and it has >50 mutations, many of which are known to affect transmissibility or cause immune escape. In this study, we sought to investigate the virological characteristics of the Omicron variant and compared it with the Delta variant which has dominated the world since mid-2021. Omicron variant replicated more slowly than the Delta variant in transmembrane serine protease 2 (TMPRSS2)-overexpressing VeroE6 (VeroE6/TMPRSS2) cells. Notably, the Delta variant replicated well in Calu3 cell line which has robust TMPRSS2 expression, while the Omicron variant replicated poorly in this cell line. Competition assay showed that Delta variant outcompeted Omicron variant in VeroE6/TMPRSS2 and Calu3 cells. To confirm the difference in entry pathway between the Omicron and Delta variants, we assessed the antiviral effect of bafilomycin A1, chloroquine (inhibiting endocytic pathway), and camostat (inhibiting TMPRSS2 pathway). Camostat potently inhibited the Delta variant but not the Omicron variant, while bafilomycin A1 and chloroquine could inhibit both Omicron and Delta variants. Moreover, the Omicron variant also showed weaker cell-cell fusion activity when compared with Delta variant in VeroE6/TMPRSS2 cells. Collectively, our results suggest that Omicron variant infection is not enhanced by TMPRSS2 but is largely mediated via the endocytic pathway. The difference in entry pathway between Omicron and Delta variants may have an implication on the clinical manifestations or disease severity.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Entry selectivity of SARS-CoV-2 variants is associated with clinical manifestation.
“suggesting entry selectivity of variants is associated with clinical manifestation [67].”
From Insights of Endocytosis Signaling in Health and Disease (2023) · cites this paper as [67]
Pharmacological inhibition of endocytic pathways potentially regressed replication of novel SARS-CoV-2 lineage B.1.1.529 (Omicron variant) in VeroE6/TMPRSS2 cell.
“Current evidence suggests that pharmacological inhibition of endocytic pathways potentially regressed replication of novel SARS-CoV-2 lineage B.1.1.529 (Omicron variant) in VeroE6/TMPRSS2 cell, suggesting entry selectivity of variants is associated with clinical manifestation [67].”
From Insights of Endocytosis Signaling in Health and Disease (2023) · cites this paper as [67]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109 · see citing works
HCA Lung Biological Network, Sungnak, W., Huang, N., Bécavin, C., Berg, M., Queen, R., Litvinukova, M., Talavera-López, C., Maatz, H., Reichart, D., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0868-6 · Cited by 2,501 · see citing works
Increased risk of SARS-CoV-2 reinfection associated with emergence of Omicron in South Africa
Pulliam, J. R. C., van Schalkwyk, C., Govender, N., Gottberg, A. V., Cohen, C., Groome, M. J., Dushoff, J., Mlisana, K., & Moultrie, H. (2021) · doi:10.1101/2021.11.11.21266068 · Cited by 1,037 · see citing works
Flagged first, then by citations
Research works printed but not linked: 22
- [1]To KK, Tsang OT, Leung WS, et al. Temporal profiles of viral load in posterior oropharyngeal saliva samples and serum antibody responses during infection by SARS-CoV-2: an observational cohort study. Lancet Infect Dis. 2020; 20: 565– 574. 32213337 PMC7158907
- [2]Chan JF, Yuan S, Kok KH, et al. A familial cluster of pneumonia associated with the 2019 novel coronavirus indicating person-to-person transmission: a study of a family cluster. Lancet. 2020; 395: 514– 523. 31986261 PMC7159286
- [4]Yeung ML, Teng JLL, Jia L, et al. Soluble ACE2-mediated cell entry of SARS-CoV-2 via interaction with proteins related to the renin-angiotensin system. Cell. 2021; 184: 2212– 28 e12. 33713620 PMC7923941
- [5]Chu H, Hu B, Huang X, et al. Host and viral determinants for efficient SARS-CoV-2 infection of the human lung. Nat Commun. 2021; 12: 134. 33420022 PMC7794309
- [6]Lempp FA, Soriaga LB, Montiel-Ruiz M, et al. Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies. Nature. 2021; 598: 342– 347. 34464958
- [7]Hoffmann M, Kleine-Weber H, Schroeder S, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020; 181: 271– 80 e8. 32142651 PMC7102627
- [8]Zhao H, To KKW, Lam H, et al. Cross-linking peptide and repurposed drugs inhibit both entry pathways of SARS-CoV-2. Nat Commun. 2021; 12: 1517. 33750821 PMC7943568
- [10]Mok BW, Liu H, Deng S, et al. Low dose inocula of SARS-CoV-2 Alpha variant transmits more efficiently than earlier variants in hamsters. Commun Biol. 2021; 4: 1102. 34545191 PMC8452646
- [11]To KK, Hung IF, Ip JD, et al. COVID-19 re-infection by a phylogenetically distinct SARS-coronavirus-2 strain confirmed by whole genome sequencing. Clin Infect Dis. 2020. doi: 10.1093/cid/ciaa1275 PMC7499500 32840608 · DOI · Paper page
- [12]Lu L, Chu AW, Zhang RR, et al. The impact of spike N501Y mutation on neutralizing activity and RBD binding of SARS-CoV-2 convalescent serum. EBioMedicine. 2021; 71: 103544. 34419925 PMC8374549
- [13]Chen LL, Lu L, Choi CY, et al. Impact of SARS-CoV-2 variant-associated RBD mutations on the susceptibility to serum antibodies elicited by COVID-19 infection or vaccination. Clin Infect Dis. 2021. doi: 10.1093/cid/ciab656 34309648 · DOI
- [16]Karim SSA, Karim QA. Omicron SARS-CoV-2 variant: a new chapter in the COVID-19 pandemic. Lancet. 2021. doi: 10.1016/S0140-6736(21)02758-6 PMC8640673 34871545 · DOI
- [17]Wong SC, Au AK, Chen H, et al. Transmission of Omicron (B.1.1.529) - SARS-CoV-2 Variant of Concern in a designated quarantine hotel for travelers: a challenge of elimination strategy of COVID-19. Lancet Reg Health West Pac 2021: 100360. doi: 10.1016/j.lanwpc.2021.100360. PMC8696199 34961854 · DOI
- [18]Shuai H, Chan JF, Yuen TT, et al. Emerging SARS-CoV-2 variants expand species tropism to murines. EBioMedicine. 2021; 73: 103643. 34689086 PMC8530107
- [19]Jackson CB, Farzan M, Chen B, et al. Mechanisms of SARS-CoV-2 entry into cells. Nat Rev Mol Cell Biol. 2021. doi: 10.1038/s41580-021-00418-x PMC8491763 34611326 · DOI
- [21]Saito A, Irie T, Suzuki R, et al. Enhanced fusogenicity and pathogenicity of SARS-CoV-2 Delta P681R mutation. Nature. 2021. doi: 10.1038/s41586-021-04266-9 PMC8828475 34823256 · DOI
- [23]Peacock TP, Goldhill DH, Zhou J, et al. The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets. Nat Microbiol. 2021; 6: 899– 909. 33907312 PMC7619196
- [24]Arora P, Sidarovich A, Kruger N, et al. B.1.617.2 enters and fuses lung cells with increased efficiency and evades antibodies induced by infection and vaccination. Cell Rep. 2021; 37: 109825. 34614392 PMC8487035
- [25]Zhang J, Xiao T, Cai Y, et al. Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant. Science. 2021; 374: 1353– 1360. 34698504 PMC10763652
- [26]Braga L, Ali H, Secco I, et al. Drugs that inhibit TMEM16 proteins block SARS-CoV-2 spike-induced syncytia. Nature. 2021; 594: 88– 93. 33827113 PMC7611055
- [27]Khan H, Winstone H, Jimenez-Guardeno JM, et al. TMPRSS2 promotes SARS-CoV-2 evasion from NCOA7-mediated restriction. PLoS Pathog. 2021; 17: e1009820. 34807954 PMC8648102
- [28]Hoffmann M, Mosbauer K, Hofmann-Winkler H, et al. Chloroquine does not inhibit infection of human lung cells with SARS-CoV-2. Nature. 2020; 585: 588– 590. 32698190
Cited by
Sorted by citations
SARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway
Willett, B. J., Grove, J., MacLean, O. A., Wilkie, C., De Lorenzo, G., Furnon, W., Cantoni, D., Scott, S., Logan, N., Ashraf, S., et al. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01143-7 · Cited by 785 · see citing works
Attenuated replication and pathogenicity of SARS-CoV-2 B.1.1.529 Omicron
Shuai, H., Chan, J. F.-W., Hu, B., Chai, Y., Yuen, T. T.-T., Yin, F., Huang, X., Yoon, C., Hu, J., Liu, H., et al. (2022) · Nature · doi:10.1038/s41586-022-04442-5 · Cited by 637 · see citing works
Self-citationSARS-CoV-2 Omicron variant: recent progress and future perspectives
Fan, Y., Li, X., Zhang, L., Wan, S., Zhang, L., & Zhou, F. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00997-x · Cited by 584 · see citing works
Pathogenicity, transmissibility, and fitness of SARS-CoV-2 Omicron in Syrian hamsters
Yuan, S., Ye, Z.-W., Liang, R., Tang, K., Zhang, A. J., Lu, G., Ong, C. P., Man Poon, V. K., Chan, C. C.-S., Mok, B. W.-Y., et al. (2022) · Science · doi:10.1126/science.abn8939 · Cited by 191 · see citing works
Self-citationOrigin, virological features, immune evasion and intervention of SARS-CoV-2 Omicron sublineages
Xia, S., Wang, L., Zhu, Y., Lu, L., & Jiang, S. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01105-9 · Cited by 164 · see citing works
Self-citationStructural and functional impact by SARS-CoV-2 Omicron spike mutations
Zhang, J., Cai, Y., Lavine, C. L., Peng, H., Zhu, H., Anand, K., Tong, P., Gautam, A. K., Mayer, M. L., Rits‐Volloch, S., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110729 · Cited by 142 · see citing works
“, 2021), but it is puzzling why it consistently shows weaker membrane fusion activity and infectivity in the form of either authentic virus or pseudovirus (Meng et al., 2021; Zeng et al., 2021; Zhao et al., 2021).”
Coronavirus Disease 2019 Disease Severity in Children Infected With the Omicron Variant
Butt, A. A., Dargham, S. R., Loka, S., Shaik, R. M., Chemaitelly, H., Tang, P., Hasan, M. R., Coyle, P. V., Yassine, H. M., Al-Khatib, H. A., et al. (2022) · Clinical Infectious Diseases · doi:10.1093/cid/ciac275 · Cited by 129 · see citing works
“[1-5] A recent VOC is the Omicron 3 variant, which, at least in adults, appears to be more infectious, perhaps because of more 4 immune evasion, than the previous variants but less likely to be associated with more severe or 5 critical disease.[6-8] For reasons that are incompletely understood, children appear less li…”
BackgroundThe omicron (B.1.1.529) SARS-CoV-2 variant of concern does not readily infect Syrian hamsters
Abdelnabi, R., Foo, C., Zhang, X., Lemmens, V., Maes, P., Slechten, B., Raymenants, J., André, E., Weynand, B., Dallmeier, K., et al. (2021) · bioRxiv · doi:10.1016/j.antiviral.2022.105253 · Cited by 129 · see citing works
“Moreover, unlike the ancestral strains and other VoCs, omicron enters cells more efficiently via the endocytic cathepsin L pathway (Peacock et al., 2022; Zhao et al., 2021).”
Bojkova, D., Widera, M., Ciesek, S., Wass, M., Michaelis, M., & Cinatl, J. (2022) · Cell Research · doi:10.1038/s41422-022-00619-9 · Cited by 123 · see citing works
Spike and nsp6 are key determinants of SARS-CoV-2 Omicron BA.1 attenuation
Chen, D. W., Chin, C. V., Kenney, D., Tavares, A. H., Khan, N., Conway, H. L., Liu, G., Choudhary, M. C., Gertje, H. P., O’Connell, A. K., et al. (2023) · Nature · doi:10.1038/s41586-023-05697-2 · Cited by 144 · see citing works
Molecular characteristics, immune evasion, and impact of SARS-CoV-2 variants
Sun, C., Xie, C., Bu, G., Zhong, L., & Zeng, M. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01039-2 · Cited by 139 · see citing works
“The viral inhibitor developed for SARS-CoV-2 mostly manifested maintained efficacy against the VOCs, significantly different from the performance of currently approved antibodies or vaccines.(258,272,313) Although non-viral specific drugs such as Camostat could theoretically avoid the mutational impact of SARS-CoV-2 v…”
BackgroundSARS-CoV-2: Evolution and Emergence of New Viral Variants
Flores-Vega, V. R., Monroy-Molina, J. V., Jiménez-Hernández, L. E., Torres, A. G., Santos, J. I., & Rosales-Reyes, R. (2022) · Viruses · doi:10.3390/v14040653 · Cited by 121 · see citing works
Guo, Y., Han, J., Zhang, Y., He, J., Yu, W., Zhang, X., Wu, J., Zhang, S., Kong, Y., Guo, Y., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.877101 · Cited by 116 · see citing works
Dhawan, M. K., Saied, A. A., Mitra, S., Alhumaydhi, F. A., Emran, T. B., & Wilairatana, P. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113522 · Cited by 127 · see citing works
“Interestingly, the Omicron variant prefers the endosomal entry route over the plasma membrane entry route, according to recent studies [66,88].”
RetractedEssential role of TMPRSS2 in SARS-CoV-2 infection in murine airways
Iwata‐Yoshikawa, N., Kakizaki, M., Shiwa-Sudo, N., Okura, T., Tahara, M., Fukushi, S., Maeda, K., Kawase, M., Asanuma, H., Tomita, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33911-8 · Cited by 108 · see citing works
Replication kinetics and infectivity of SARS-CoV-2 variants of concern in common cell culture models
Mautner, L., Hoyos, M., Dangel, A., Berger, C., Ehrhardt, A., & Baiker, A. E. (2022) · Virology Journal · doi:10.1186/s12985-022-01802-5 · Cited by 104 · see citing works
“We hope that this data provides support for researchers worldwide in their experimental design for work on SARS-CoV-2 such as performing virus isolation and propagation on Vero E6 while conducting infection studies or drug screening and antibody-based assays rather on the human cell lines Caco-2 and Calu-3.”
BackgroundInfluentialAggarwal, A., Akerman, A., Milogiannakis, V., Silva, M., Walker, G., Stella, A., Kindinger, A., Angelovich, T., Waring, E., Amatayakul-Chantler, S., et al. (2022) · medRxiv · doi:10.1016/j.ebiom.2022.104270 · Cited by 98 · see citing works
Armando, F., Beythien, G., Kaiser, F., Allnoch, L., Heydemann, L., Rosiak, M., Becker, S. O., González-Hernández, M., Lamers, M., Haagmans, B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31200-y · Cited by 95 · see citing works
SARS-CoV-2 requires acidic pH to infect cells
Kreutzberger, A. J. B., Sanyal, A., Saminathan, A., Bloyet, L.-M., Stumpf, S. D., Liu, Z., Ojha, R., Patjas, M. T., Geneid, A., Scanavachi, G., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2209514119 · Cited by 94 · see citing works
Fall, A., Eldesouki, R. E., Sachithanandham, J., Morris, C. P., Norton, J. M., Gaston, D. C., Forman, M., Abdullah, O. R., Gallagher, N., Li, M., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104008 · Cited by 144 · see citing works
Schubert, M., Bertoglio, F., Steinke, S., Heine, P. A., Ynga-Durand, M. A., Maaß, H., Sammartino, J. C., Cassaniti, I., Zuo, F., Du, L., et al. (2022) · BMC Medicine · doi:10.1186/s12916-022-02312-5 · Cited by 91 · see citing works
“Omicron, it was shown that the cell binding is reduced (weaker cell-cell fusion activity) when comparing Omicron to Delta [33].”
ResultPastorio, C., Zech, F., Noettger, S., Jung, C., Jacob, T., Sanderson, T., Sparrer, K. M. J., & Kirchhoff, F. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.07.006 · Cited by 90 · see citing works
The puzzling mutational landscape of the SARS‐2‐variant Omicron
Fantini, J., Yahi, N., Colson, P., Chahinian, H., Scola, B. L., & Raoult, D. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27577 · Cited by 80 · see citing works
“In some cells, the infectivity and replication of the omicron variant were higher than delta, whereas in other cells opposite results were obtained, with delta being clearly more performant than omicron.(14,15) Moreover, several reports suggest that the omicron variant spike confers impaired cell–cell fusion activity,…”
ResultSARS-CoV-2 and innate immunity: the good, the bad, and the “goldilocks”
Sievers, B. L., Cheng, M. T. K., Csiba, K., Meng, B., & Gupta, R. K. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-023-01104-y · Cited by 85 · see citing works
“This suggests that different SARS-CoV-2 variants have different sensitivities to the TMPRSS2-mediated entry pathway; thus, they may have different susceptibility to antiviral IFITMs [73, 82, 83].”
BackgroundSpike mutations contributing to the altered entry preference of SARS-CoV-2 omicron BA.1 and BA.2
Hu, B., Chan, J. F., Liu, H., Liu, Y., Chai, Y., Shi, J., Shuai, H., Hou, Y., Huang, X., Yuen, T. T., et al. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2022.2117098 · Cited by 77 · see citing works
“…(VOCs) [12–14], which is contributed by the unique virological features of Omicron BA.1 in com - parison to other SARS-CoV-2 strains, including less efficient transmembrane serine protease 2 (TMPRSS2) usage, less spike cleavage, lower fusogenicity, and an altered entry mechanism [12,14–18].”
Self-citationPinato, D., J. Aguilar-Company, Ferrante, D., Hanbury, G., Bower, M., Salazar, R., Mirallas, O., Sureda, A., Plaja, A., Cucurull, M., et al. (2022) · The Lancet Oncology · doi:10.1016/s1470-2045(22)00273-x · Cited by 74 · see citing works
Chiu, M. C., Li, C., Liu, X., Song, W., Wan, Z., Yu, Y., Huang, J., Xiao, D., Chu, H., Cai, J., et al. (2022) · mBio · doi:10.1128/mbio.01944-22 · Cited by 72 · see citing works
“S1A and B), which was repeatedly demonstrated in other studies using cell lines (43), highlighting the strength of biologically relevant nasal organoids.”
BackgroundSelf-citationPitts, J., Li, J., Perry, J. K., Pont, V. D., Riola, N. C., Rodriguez, L., Lu, X., Kurhade, C., Xie, X., Camus, G., et al. (2022) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00222-22 · Cited by 72 · see citing works
“Due to the low absorbance signal observed with the Omicron variant at the standard 48-h time point, likely stemming from the reduced in vitro replication efficiency of Omicron (34), the assay was also extended to 72 h and compared with WA1 assessed at the same time point.”
MethodLysosomal enzyme trafficking: from molecular mechanisms to human diseases.
Braulke, T., Carette, J., & Palm, W. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.06.005 · Cited by 65 · see citing works
Insights of Endocytosis Signaling in Health and Disease
Pathak, C., Vaidya, F. U., Waghela, B. N., Jaiswara, P. K., Gupta, V. K., Kumar, A., Rajendran, B. K., & Ranjan, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032971 · Cited by 59 · see citing works
“529 (Omicron variant) in VeroE6/TMPRSS2 cell, suggesting entry selectivity of variants is associated with clinical manifestation [67].”
BackgroundButt, A. A., Dargham, S. R., Tang, P., Chemaitelly, H. S., Hasan, M. R., Coyle, P. V., Kaleeckal, A. H., Latif, A. N., Loka, S., Shaik, R. M., et al. (2022) · Journal of Global Health · doi:10.7189/jogh.12.05032 · Cited by 58 · see citing works
Coronavirus Infection and Cholesterol Metabolism
Dai, J., Wang, H., Liao, Y., Tan, L., Sun, Y., Song, C., Liu, W., Qiu, X., & Ding, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.791267 · Cited by 67 · see citing works
Butowt, R., Bilińska, K., & von Bartheld, C. S. (2022) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiac113 · Cited by 71 · see citing works
Spike protein mediated membrane fusion during SARS‐CoV‐2 infection
Li, X., Yuan, H., Li, X., & Wang, H. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28212 · Cited by 70 · see citing works
“increased transmissibility, its S protein has been shown to have a reduced ability to induce the formation of syncytia.(111,112) On the”
BackgroundZhou, H., Møhlenberg, M., Thakor, J. C., Tuli, H. S., Wang, P., Assaraf, Y. G., Dhama, K., & Jiang, S. (2022) · Clinical Microbiology Reviews · doi:10.1128/cmr.00014-22 · Cited by 76 · see citing works
Medigeshi, G., Batra, G., Murugesan, D. R., Thiruvengadam, R., Chattopadhyay, S., Das, B., Gosain, M., Ayushi, Singh, J., Anbalagan, A., et al. (2022) · medRxiv · doi:10.1016/j.ebiom.2022.103938 · Cited by 57 · see citing works
Mykytyn, A. Z., Breugem, T. I., Geurts, M. H., Beumer, J., Schipper, D., van Acker, R., van den Doel, P. B., van Royen, M. E., Zhang, J., Clevers, H. C., et al. (2023) · Journal of Virology · doi:10.1128/jvi.00851-23 · Cited by 58 · see citing works
Tiecco, G., Storti, S., Antoni, M. D., Focà, E., Castelli, F., & Quirós-Roldán, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23041987 · Cited by 58 · see citing works
“This observation supports the point that the Omicron variant infection is not enhanced by TMPRSS2 but is largely mediated by the endocytic pathway instead [14].”
BackgroundResultUnderstanding COVID-19 in children: immune determinants and post-infection conditions
Rotulo, G. A., & Palma, P. (2023) · Pediatric Research · doi:10.1038/s41390-023-02549-7 · Cited by 59 · see citing works
“In particular, Omicron’s spike protein requires the activity of endosomal cathepsins to be cleaved, while it is unable to efficiently use the cellular protease TMPRSS2.”
BackgroundArora, P., Zhang, L., Krüger, N., Rocha, C., Sidarovich, A., Schulz, S. R., Kempf, A. M., Graichen, L., Moldenhauer, A.-S., Cossmann, A., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.04.017 · Cited by 44 · see citing works
“…fusion and syncytia formation was previously found to be reduced, whereas the S protein of the Delta variant (B.1.617.2) was reported to exhibit increased capacity to mediate cell-cell fusion (Arora et al., 2021;Meng et al., 2022; Saito et al., 2022; Suzuki et al., 2022; Zhao et al., 2022).”
InfluentialSARS-CoV-2 spike protein: structure, viral entry and variants
Chen, B., Farzan, M., & Choe, H. (2025) · Nature Reviews Microbiology · doi:10.1038/s41579-025-01185-8 · Cited by 54 · see citing works
“…Omicron subvariants (for example, BA.1) seem to use TMPRSS2 less and depend more on the endocytic entry than the pre-Omicron variants 73–75 , possibly leading to a change in cellular tropism away from TMPRSS2-expressing cells, and explaining the altered tissue tropism and pathogenesis 73,74,76,77 .”
Oral Pathology in COVID-19 and SARS-CoV-2 Infection—Molecular Aspects
Droździk, A., & Droździk, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031431 · Cited by 63 · see citing works
“As a consequence, the Omicron variant replicates more slowly than the Delta variant in cells overexpressing TMPRSS2 [50], with a possibly reduced cytopathic effect.”
BackgroundShi, G., Li, T., Lai, K. K., Johnson, R. F., Yewdell, J. W., & Compton, A. A. (2024) · Nature Communications · doi:10.1038/s41467-024-45075-8 · Cited by 45 · see citing works
Global impact of delta plus variant and vaccination
Chavda, V., & Apostolopoulos, V. (2022) · Expert Review of Vaccines · doi:10.1080/14760584.2022.2044800 · Cited by 46 · see citing works
“cell-cell fusion activity when compared with Delta variant in VeroE6/TMPRSS2 cells [28].”
Cheng, V. C., Lung, D. C., Wong, S., Au, A. K.-W., Wang, Q., Chen, H., Li, X., Chu, A. W., Ip, J. D., Chan, W.-M., et al. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.128504 · Cited by 41 · see citing works
Self-citationRecent insights into SARS‐CoV‐2 omicron variant
da Silva, S. J. R., Kohl, A., Pena, L., & Pardee, K. (2022) · Reviews in Medical Virology · doi:10.1002/rmv.2373 · Cited by 54 · see citing works
“viral replication of the omicron variant and compared it with the delta variant.(22) This work showed that the omicron variant replicated more slowly than the delta variant in transmembrane serine protease 2 (TMPRSS2)‐overexpressing VeroE6 (VeroE6/TMPRSS2) cells, which provides an interesting way to evaluate the pathw…”
BackgroundResultSuryawanshi, R., Chen, I. P., Ma, T., Syed, A. M., Simoneau, C., Ciling, A., Khalid, M., Sreekumar, B., Chen, P.-Y., George, A. F., et al. (2022) · medRxiv · doi:10.1101/2022.01.13.22269243 · Cited by 45 · see citing works
Molecular insights into the adaptive evolution of SARS-CoV-2 spike protein
Yao, Z., Zhang, L., Duan, Y., Tang, X., & Lü, J. (2024) · Journal of Infection · doi:10.1016/j.jinf.2024.106121 · Cited by 46 · see citing works
Sohan, M., Hossain, M. J., & Islam, M. R. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27574 · Cited by 44
“November 2021, has prompted worldwide fear due to its contagiousness and immunity escaping capacity.(1,2) Omicron has gotten a”
BackgroundLiterature Review of Omicron: A Grim Reality Amidst COVID-19
Arora, S., Grover, V., Saluja, P., Algarni, Y. A., Saquib, S. A., Asif, S. M., Batra, K., Alshahrani, M. Y., Das, G., Jain, R., et al. (2022) · Microorganisms · doi:10.3390/microorganisms10020451 · Cited by 53 · see citing works
“Recent studies have reported that Omicron has a different mechanism for entering the host, and is capable of gaining cell entry independent of the transmembrane serine protease 2 (TMPRSS2) [24].”
BackgroundIs Booster Dose Strategy Sufficient for Omicron Variant of SARS-CoV-2?
Chavda, V. P., & Apostolopoulos, V. (2022) · Vaccines · doi:10.3390/vaccines10030367 · Cited by 50 · see citing works
“As such, the Spike protein is used in most currently approved vaccines, however, significant concerns about Omicron’s enhanced transmissibility and immune escape have been raised [13].”
BackgroundSARS‐CoV‐2 Omicron and its current known unknowns: A narrative review
Le, T. T. B., Vasanthakumaran, T., Hau, N. T. H., Hung, I., Luu, M. N., Khan, Z. A., An, N. T., Tran, V. P., Lee, W. J., Aziz, J. M. A., et al. (2022) · Reviews in Medical Virology · doi:10.1002/rmv.2398 · Cited by 41 · see citing works
Fall, A., Eldesouki, R., Sachithanandham, J., Morris, C., Norton, J., Gaston, D. C., Forman, M., Abdullah, O., Gallagher, N., Li, M., et al. (2022) · medRxiv · doi:10.1101/2022.01.26.22269927 · Cited by 39
“The slower viral growth might indicate an 302 alternative entry pathway that is less dependent on TMPRSS2 (27).”
InfluentialOmicron subvariant BA.5 efficiently infects lung cells
Hoffmann, M., Wong, L.-Y. R., Arora, P., Zhang, L., Rocha, C., Odle, A. E., Nehlmeier, I., Kempf, A. M., Richter, A. M., Halwe, N. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39147-4 · Cited by 38 · see citing works
Mayr, F., Talisa, V., Castro, A. D., Shaikh, O., Omer, S. B., & Butt, A. (2022) · Nature Communications · doi:10.1038/s41467-022-31402-4 · Cited by 38
Evolution of nasal and olfactory infection characteristics of SARS-CoV-2 variants
Chen, M., Pekosz, A. S., Villano, J., Shen, W., Zhou, R., Kulaga, H. M., Li, Z., Smith, A. K., Gurung, A., Beck, S. E., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci174439 · Cited by 47 · see citing works
“The decreased olfactory tropism in the Omicron variant is consistent with the recently reported endocytic entry pathway (26, 27).”
Yamamoto, M., Tomita, K., Hirayama, Y., Inoue, J., Kawaguchi, Y., & Gohda, J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.21.485084 · Cited by 34 · see citing works
“Omicron variant displays poor syncytium formation mediated by metalloproteinases without affecting the S1/S2 cleavage of its S protein Reduced syncytia formation through the TMPRSS2 pathway has been reported in Omicron, suggesting a correlation with lower pathogenicity [2, 10, 12, 13].”
InfluentialInfluence of immune escape and nasopharyngeal virus load on the spread of SARS-CoV-2 Omicron variant
Migueres, M., Diméglio, C., Trémeaux, P., Abravanel, F., Raymond, S., Lhomme, S., Mansuy, J., & Izopet, J. (2022) · Journal of Infection · doi:10.1016/j.jinf.2022.01.036 · Cited by 36
Functional properties of the spike glycoprotein of the emerging SARS-CoV-2 variant B.1.1.529
Wang, Q., Anang, S., Iketani, S., Guo, Y., Liu, L., Katsamba, P. S., Shapiro, L. S., Ho, D. D., & Sodroski, J. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110924 · Cited by 32 · see citing works
“529 S glycoprotein predominantly occurs through the use of endosomal cathepsins, consistent with other reports (Meng et al., 2022; Zhao et al., 2022).”
Hydroxychloroquine blocks SARS-CoV-2 entry into the endocytic pathway in mammalian cell culture
Yuan, Z., Pavel, M. A., Wang, H., Kwachukwu, J. C., Mediouni, S., Jablonski, J. A., Nettles, K. W., Reddy, C. B., Valente, S. T., & Hansen, S. B. (2022) · Communications Biology · doi:10.1038/s42003-022-03841-8 · Cited by 50 · see citing works
Covid-19: is omicron less lethal than delta?
Lorenzo-Redondo, R., Ozer, E. A., & Hultquist, J. (2022) · British medical journal · doi:10.1136/bmj.o1806 · Cited by 34
SARS-CoV-2 Variants of Concern Hijack IFITM2 for Efficient Replication in Human Lung Cells
Nchioua, R., Schundner, A., Kmieć, D., Bozzo, C. P., Zech, F., Koepke, L., Graf, A., Krebs, S., Blum, H., Frick, M., et al. (2022) · Journal of Virology · doi:10.1128/jvi.00594-22 · Cited by 36 · see citing works
Antiviral Molecular Targets of Essential Oils against SARS-CoV-2: A Systematic Review
Iqhrammullah, M., Rizki, D., Purnama, A., Duta, T. F., Harapan, H., Idroes, R., & Ginting, B. (2023) · Scientia Pharmaceutica · doi:10.3390/scipharm91010015 · Cited by 33 · see citing works
“replication and fusion activities in TMPRSS2-expressing cells, such as in Omicron; the activities are lower compared to the Delta variant [60].”
BackgroundTang, C. Y., Boftsi, M., Staudt, L., McElroy, J., Li, T., Duong, S., Ohler, A., Ritter, D., Hammer, R. D., Hang, J., et al. (2022) · Virology · doi:10.1016/j.virol.2022.09.009 · Cited by 33
Revealing the mystery of persistent smell loss in long COVID patients
Park, J. W., Wang, X., & Xu, R. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.73485 · Cited by 36 · see citing works
“Early estimation indicates that Omicron is less severe than the previous variants, possibly due to its less efficient viral replication [5, 6].”
BackgroundStrohl, W. R., Ku, Z., An, Z., Carroll, S. F., Keyt, B. A., & Strohl, L. M. (2022) · BioDrugs · doi:10.1007/s40259-022-00529-7 · Cited by 34 · see citing works
Deng, J., Ma, Y., Liu, Q., Du, M., Liu, M., & Liu, J. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph192315932 · Cited by 37 · see citing works
“In vitro experiments have also shown that Omicron has lower replication and fusion activity than Delta [42].”
BackgroundAntigenic evolution of SARS coronavirus 2
Mykytyn, A. Z., Fouchier, R. A. M., & Haagmans, B. L. (2023) · Current Opinion in Virology · doi:10.1016/j.coviro.2023.101349 · Cited by 36 · see citing works
Zhang, Y., Almazi, J. G., Ong, H. X., Johansen, M. D., Ledger, S., Traini, D., Hansbro, P. M., Kelleher, A. D., & Ahlenstiel, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052408 · Cited by 31 · see citing works
“Particularly, Paxlovid might have therapeutic potential in the newly emerging Omicron variant [10], which is fundamentally different from previous VOC, as it does not appear to use the TMPRSS2 protease co-receptor [11,12] or target the lung as effectively as previous ones [13–17].”
BackgroundSpike protein-independent attenuation of SARS-CoV-2 Omicron variant in laboratory mice
Liu, S., Selvaraj, P., Sangare, K., Luan, B., & Wang, T. T. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111359 · Cited by 28 · see citing works
“In support, the Omicron spike is less fusogenic compared with that of the Delta variant (Cong Zeng et al., 2021; Zhao et al., 2021).”
Wang, L., Wang, S., Wu, L., Li, W., Bray, W. A., Clark, A. E., Gonzalez, G. M., Wang, Y., Carlin, A. F., & Rana, T. M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210361120 · Cited by 34 · see citing works
“Interestingly, a possible explanation for the latter observation comes from two recent studies suggesting that Omicron is less dependent than other SARS-CoV-2 strains on TMPRSS2 for cell infection (27, 28).”
ResultSARS-CoV-2 variants: Impact on biological and clinical outcome
Mahilkar, S., Agrawal, S. R., Chaudhary, S., Parikh, S., Sonkar, S. C., Verma, D. K., Chitalia, V., Mehta, D., Koner, B. C., Vijay, N., et al. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.995960 · Cited by 35 · see citing works
“The difference in entry pathways between the Omicron and Delta variants may have an implication on the clinical manifestations or disease severity (95).”
BackgroundZhu, Y., Chew, K., Wu, M., Karawita, A., McCallum, G., Steele, L. E., Yamamoto, A., Labzin, L. I., Yarlagadda, T., Khromykh, A., et al. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001728 · Cited by 30
“These data support suggestions that Omicron does not necessarily have a replicative advantage over Delta in the URT of adults [33], and the observed increase in transmission with Omicron in adults is more likely reflective of increased antibody evasion [34–37].”
Vardhan, S., & Sahoo, S. K. (2022) · Comput. Biol. Medicine · doi:10.1016/j.compbiomed.2022.105367 · Cited by 30 · see citing works
Stewart, R., Yan, K., Ellis, S. A., Bishop, C. R., Dumenil, T. D., Tang, B., Nguyen, W., Larcher, T., Parry, R. H., Sng, J. D. J., et al. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1320856 · Cited by 32 · see citing works
Endomembrane remodeling in SARS-CoV-2 infection
Chen, D., Zhao, Y. G., & Zhang, H. (2022) · Cell Insight · doi:10.1016/j.cellin.2022.100031 · Cited by 32 · see citing works
“The entry of Omicron mainly depends on the endocytic pathway, and compared to the Delta variant it thus exhibits lower infectivity in cells expressing high levels of TMPRSS2, and less sensitivity to the TMPRSS2 inhibitor Camostat (Meng et al., 2022; Zhao et al., 2022).”
Fantini, J., Chahinian, H., & Yahi, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031923 · Cited by 26 · see citing works
“infectio kinetics comparing the Delta and Omicron in Calu-3 cells, which have high level expressions of TMPRSS2 and in (TMPRSS2)-overexpressing VeroE6 cells [70].”
BackgroundInfluentialZhang, Z., Hao, M., Zhang, X.-C., He, Y.-F., Chen, X.-S., Taylor, E., & Zhang, J. (2022) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2022.12.012 · Cited by 26 · see citing works
Comparison of clinical characteristics of wild-type SARS-CoV-2 and Omicron
Kırca, F., Aydoğan, S., Gözalan, A., Kayıpmaz, A., Özdemir, F. A. E., Tekçe, Y., Beşer, İ. O., Gun, P., Ökten, R. S., & Dinç, B. (2022) · Revista da Associação Médica Brasileira · doi:10.1590/1806-9282.20220880 · Cited by 26
Alterations in SARS-CoV-2 Omicron and Delta peptides presentation by HLA molecules
Nersisyan, S. A., Zhiyanov, A., Zakharova, M., Ishina, I. A., Kurbatskaia, I. N., Mamedov, A. E., Galatenko, A. V., Shkurnikov, M. Y., Gabibov, A. G., & Tonevitsky, A. (2022) · PeerJ · doi:10.7717/peerj.13354 · Cited by 28 · see citing works
Yuan, S.-F., Ye, Z.-W., Liang, R., Tang, K., Zhang, A., Lu, G., Ong, C., Poon, V., Chan, C., Mok, B.-B. W., et al. (2022) · bioRxiv · doi:10.1101/2022.01.12.476031 · Cited by 26 · see citing works
“In human lung-derived Calu-3 cells, the Omicron variant shows 200 lower replication than the Delta variant and D614G strain in in pseudovirus and/or live virus 201 assays (21,27).”
BackgroundSelf-citationAlpha-1-antitrypsin and its variant-dependent role in COVID-19 pathogenesisPreprint
Stevens, C. S., Oguntuyo, K. Y., Kowdle, S., Brambilla, L., Haas, G. D., Gowlikar, A., Siddiquey, M. N. A., Schilke, R. M., Woolard, M. D., Zhang, H., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.14.248880 · Cited by 33 · see citing works
“While many similarities exist between all variants of concern (VOCs), some 247 show distinct differences, particularly in viral entry and proteolytic processing of Spike 248 (4, 22, 25).”
SARS-CoV-2 Omicron (B.1.1.529) Variant: A Challenge with COVID-19
Afshar, Z. M., Pirzaman, A. T., Karim, B., Anaraki, S. R., Hosseinzadeh, R., Pireivatlou, E. S., Babazadeh, A., Hosseinzadeh, D., Miri, S. R., Sio, T. T. W., et al. (2023) · Diagnostics · doi:10.3390/diagnostics13030559 · Cited by 29 · see citing works
Performance of nasopharyngeal swab and saliva in detecting Delta and Omicron SARS‐CoV‐2 variants
Uršič, T., Kogoj, R., Šikonja, J., Roškarič, D., Virant, M. J., Bogovič, P., & Petrovec, M. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27898 · Cited by 25 · see citing works
“These findings could also be explained by evidence of less efficient replication and fusion activity of Omicron when compared with Delta variant in TMPRSS2‐expressed cells, which could be the reason for less severe lung pathology.(26,31) Although the results between NPS and saliva in the Delta wave were highly concord…”
ResultTherapeutics to Tackle Omicron Outbreak
Chavda, V. P., Ghali, E. N. H. K., Yallapu, M. M., & Apostolopoulos, V. (2022) · Immunotherapy · doi:10.2217/imt-2022-0064 · Cited by 31 · see citing works
“The viral replication of the Omicron variant is through an endocytic pathway rather than the transmembrane serine protease 2 pathway as that of other variants of concern [22].”
BackgroundSub‐lineages of the SARS‐CoV‐2 Omicron variants: Characteristics and prevention
Xu, A., Hong, B., Lou, F., Wang, S., Li, W., Shafqat, A., An, X., Zhao, Y., Song, L., Tong, Y., et al. (2022) · MedComm · doi:10.1002/mco2.172 · Cited by 28 · see citing works
Zhao, H., Meng, X., Peng, Z., Lam, H., Zhang, C., Zhou, X., Chan, J. F., Kao, R. Y. T., To, K. K., & Yuen, K. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2022.2051753 · Cited by 26 · see citing works
“not on TMPRSS2 for viral replication [30].”
Self-citationDergaa, I., Musa, S., Romdhani, M., Souissi, A., Abdulmalik, M., Chamari, K., & Saad, H. B. (2022) · Biology of Sport · doi:10.5114/biolsport.2022.113293 · Cited by 24
“If we take the example of the Omicron strain, the virus evolved in a way that it became highly contagious and less severe compared to previous variants [33].”
ResultPhenotypic evolution of SARS-CoV-2 spike during the COVID-19 pandemic
Furnon, W., Cowton, V. M., Lorenzo, G. D., Orton, R. J., Herder, V., Cantoni, D. M., Ilia, G., Mendonça, D. C., Kerr, K., Allan, J., et al. (2025) · Nature Microbiology · doi:10.1038/s41564-024-01878-5 · Cited by 23 · see citing works
Interferon‐inducible phospholipids govern IFITM3‐dependent endosomal antiviral immunity
Unali, G., Crivicich, G., Pagani, I., Abou-Alezz, M., Folchini, F., Valeri, E., Matafora, V., Reisz, J., Giordano, A., Cuccovillo, I., et al. (2023) · EMBO Journal · doi:10.15252/embj.2022112234 · Cited by 23 · see citing works
“In agreement with a recently proposed endosomal entry mechanism for the recent SARS-CoV2 Omicron variant (Pia & Rowland-Jones, 2022; Zhao et al, 2022), Omicron Spike-gp-pseudotyped LV were susceptible to both IFITM1 and IFITM3 in Calu3 cells (Fig 7G), and replicating SARS-CoV2 Omicron was mostly…”
BackgroundShi, J., Zheng, J., Tai, W.-B., Verma, A. K., Zhang, X., Geng, Q., Wang, G., Guan, X., Malisheni, M., Odle, A. E., et al. (2022) · Journal of Virology · doi:10.1128/jvi.00118-22 · Cited by 22 · see citing works
Islam, M. R., Nasreen, W., Anjum, R., Shahriar, M., Roy, A., Dhama, K., & Bhuiyan, M. A. (2022) · Clinical Pathology · doi:10.1177/2632010x221124908 · Cited by 22
Hu, C. (2024) · Natural Products and Bioprospecting · doi:10.1007/s13659-024-00432-4 · Cited by 24 · see citing works
“…[152], a combination of BRII-196/ BRII-198 [153], as well as healthy E(e)SEEDi lifestyle [70, 71] and better nutrient strategies [154–158], will help to combat the infection of SARS-CoV-2 and its major variants (Delta, Omicron, and XBB) [159–161], thus, combat finally the COVID-19 infection.”
BackgroundLeidi, F., Boari, G., Scarano, O., Mangili, B., Gorla, G., Corbani, A., Accordini, B., Napoli, F., Ghidelli, C., Archenti, G., et al. (2022) · Internal and Emergency Medicine · doi:10.1007/s11739-022-03034-5 · Cited by 21
“Therefore, such an impressive decrease in mortality in a non-vaccinated population may be fully explained not only by the factors reported above (i.e. early diagnosis and hospitalization and improvement of the hospital treatment and care) but maybe also by a progressive reduction of SARS-CoV-2 lethality, in line with…”
Omicron BA.2 Lineage, the “Stealth” Variant: Is It Truly a Silent Epidemic? A Literature Review
Tiecco, G., Storti, S., Arsuffi, S., Degli-Antoni, M., Focà, E., Castelli, F., & Quiros-Roldan, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137315 · Cited by 21 · see citing works
“However, in vitro entry assay studies state that Omicron variant infection is not enhanced by TMPRSS2, and no particular difference has been seen between Delta and Omicron entry that might explain the overtake of Delta by Omicron [35].”
BackgroundWang, S., Ran, W., Sun, L., Fan, Q., Zhao, Y., Wang, B., Yang, J., He, Y., Wu, Y. T., Wang, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48503-x · Cited by 21 · see citing works
Self-citationBeaudoin, C. A., Pandurangan, A., Kim, S. Y., Hamaia, S., Huang, C. L.-H., Blundell, T., Vedithi, S., & Jackson, A. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27845 · Cited by 20 · see citing works
Intra- vs. Interhost Evolution of SARS-CoV-2 Driven by Uncorrelated Selection—The Evolution Thwarted
Hou, M., Shi, J., Gong, Z., Wen, H.-J., Lan, Y., Deng, X.-Z., Fan, Q., Li, J.-J., Jiang, M.-L., Tang, X., et al. (2023) · Molecular biology and evolution · doi:10.1093/molbev/msad204 · Cited by 19 · see citing works
“Also, Omicron is more infectious than Delta but has a lower viral load than Delta (Puhach et al. 2022), even in rhesus macaque (van Doremalen et al. 2022).”
BackgroundInfluentialGajula, S. N. R., Khairnar, A. S., Jock, P., Kumari, N., Pratima, K., Munjal, V., Kalan, P., & Sonti, R. (2023) · Expert Review of Proteomics · doi:10.1080/14789450.2023.2191845 · Cited by 23 · see citing works
“mainland China to achieve their Zero Covid strategy [4].”
BackgroundA trifunctional peptide broadly inhibits SARS-CoV-2 Delta and Omicron variants in hamsters
Zhao, H.-J., To, K., Lam, H.-Y., Zhang, C., Peng, Z., Meng, X.-J., Wang, X.-K., Zhang, A., Yan, B., Cai, J.-P., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00428-9 · Cited by 19
Self-citation
- Authors
- Zhao, H., Lu, L., Peng, Z., Chen, L.-L., Meng, X., Zhang, C., Ip, J. D., Chan, W.-M., Chu, A. W.-H., Chan, K.-H., Jin, D.-Y., Chen, H., Yuen, K.-Y., & To, K. K.-W.
- Affiliations
- University of Hong Kong (HK)
- Queen Mary Hospital (CN)
- Corresponding author
- Zhao, Hanjun
- To, Kelvin Kai-Wang
- ORCID
- Venue
- Emerging Microbes & Infections
- Publisher
- Informa UK Limited
- Published
- 2022-01-19
- Volume
- 11
- Issue
- 1
- Pages
- 277-283
- ISSN
- 2222-1751 (ISSN-L)
- PMC
- PMC8774049
- OpenAlex
- W4200625712
- Cited by
- 413
- References
- 25
- Citations by year
- 2026: 12 · 2025: 29 · 2024: 68 · 2023: 104 · 2022: 197 · 2021: 2 · 2020: 1
- FWCI
- 29.38
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Emerging Microbes & Infections (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Theme-Based Research Scheme (T11-709/21-N)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Infectious Diseases › COVID-19 Clinical Research Studies
- Physical Sciences › Mathematics › Modeling and Simulation › COVID-19 epidemiological studies
- Keywords
- Omicron variant, Delta variant, viral entry pathways, TMPRSS2, endocytic pathway, viral replication, cell-cell fusion, camostat, bafilomycin A1, chloroquine, competition assay
- MeSH terms
- Whole Genome Sequencing, COVID-19, SARS-CoV-2, Animals, Carcinoma, Non-Small-Cell Lung, Chlorocebus aethiops, Chloroquine, Endocytosis, Esters, Guanidines, Humans, Lung Neoplasms, Recombinant Proteins, Serine Endopeptidases, Vero Cells, Virus Cultivation, Virus Replication, Macrolides, Cell Line, Tumor, Virus Internalization, Immune Evasion
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
