Broadly neutralizing hemagglutinin stalk–specific antibodies require FcγR interactions for protection against influenza virus in vivo
Open accessAbstract
Neutralizing antibodies against influenza viruses have traditionally been thought to provide protection exclusively through their variable region; the contributions of mechanisms conferred by the Fc domain remain controversial. We investigated the in vivo contributions of Fc interactions with their cognate receptors for a collection of neutralizing anti-influenza antibodies. Whereas five broadly neutralizing monoclonal antibodies (bNAbs) targeting the conserved stalk region of hemagglutinin (HA) required interactions between the antibody Fc and Fc receptors for IgG (FcγRs) to confer protection from lethal H1N1 challenge, three strain-specific monoclonal Abs (mAbs) against the variable head domain of HA were equally protective in the presence or absence of FcγR interactions. Although all antibodies blocked infection, only anti-stalk bNAbs were capable of mediating cytotoxicity of infected cells, which accounts for their FcγR dependence. Immune complexes generated with anti-HA stalk mAb efficiently interacted with FcγRs, but anti-HA head immune complexes did not. These results suggest that FcγR binding capacity by anti-HA antibodies was dependent on the interaction of the cognate Fab with antigen. We exploited these disparate mechanisms of mAb-mediated protection to reengineer an anti-stalk bNAb to selectively enhance FcγR engagement to augment its protective activity. These findings reveal a previously uncharacterized property of bNAbs and guide an approach toward enhancing mAb-mediated antiviral therapeutics.
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?
T cells are important in the host response to SARS-CoV-2 by killing infected cells, helping B cells and antibody production, and possibly lowering the risk of vaccine-induced enhanced disease.
“As expected for a viral infection, T cells are also important mediators in the host response to SARS-CoV-2 infection, by killing infected cells, supporting B cell function and antibody responses, and, possibly, reducing the risk of vaccine-induced enhanced disease39,40”
From Immunological mechanisms of vaccine-induced protection against COVID-19 in humans (2021) · cites this paper as [39]
Non-neutralizing binding antibodies have shown protective effects in many viral infections.
“Binding, non-neutralizing antibodies have also been shown to have a protective effect in many viral infections (Asthagiri Arunkumar et al., 2019; DiLillo et al., 2014; Saphire et al., 2018)”
From SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2 (2021) · cites this paper as DiLillo et al., 2014
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
Pushko, P., Pumpens, P., & Grens, E. (2013) · Intervirology · doi:10.1159/000346773 · Cited by 5,970 · see citing works
Fcγ receptors as regulators of immune responses
Nimmerjahn, F., & Ravetch, J. V. (2008) · Nature Reviews Immunology · doi:10.1038/nri2206 · Cited by 2,947 · see citing works
Self-citationInhibitory Fc receptors modulate in vivo cytoxicity against tumor targets
Clynes, R. A., Towers, T. L., Presta, L. G., & Ravetch, J. V. (2000) · Nature Medicine · doi:10.1038/74704 · Cited by 2,768 · see citing works
Self-citationReceptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin
Skehel, J. J., & Wiley, D. C. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.531 · Cited by 2,706 · see citing works
Wiley, D. C., Wilson, I. A., & Skehel, J. J. (1981) · Nature · doi:10.1038/289373a0 · Cited by 1,623 · see citing works
CD107a as a functional marker for the identification of natural killer cell activity
Alter, G., Malenfant, J., & Altfeld, M. A. (2004) · Journal of Immunological Methods · doi:10.1016/j.jim.2004.08.008 · Cited by 1,416 · see citing works
Antibody Recognition of a Highly Conserved Influenza Virus Epitope
Ekiert, D. C., Bhabha, G., Elsliger, M.-A., Friesen, R. H. E., Jongeneelen, M., Throsby, M., Goudsmit, J., & Wilson, I. A. (2009) · Science · doi:10.1126/science.1171491 · Cited by 1,326 · see citing works
Corti, D., Voss, J., Gamblin, S. J., Codoni, G., Macagno, A., Jarrossay, D., Vachieri, S. G., Pinna, D., Minola, A., Vanzetta, F., et al. (2011) · Science · doi:10.1126/science.1205669 · Cited by 1,203 · see citing works
Sui, J., Hwang, W. C., Perez, S., Ge, W., Aird, D. R., Chen, L., Santelli, E., Stec, B., Cadwell, G., Ali, M., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1566 · Cited by 1,132 · see citing works
Divergent Immunoglobulin G Subclass Activity Through Selective Fc Receptor Binding
Nimmerjahn, F., & Ravetch, J. V. (2005) · Science · doi:10.1126/science.1118948 · Cited by 1,040 · see citing works
Self-citationFcR γ chain deletion results in pleiotrophic effector cell defects
Takai, T., Li, M., Sylvestre, D. L., Clynes, R., & Ravetch, J. V. (1994) · Cell · doi:10.1016/0092-8674(94)90115-5 · Cited by 951 · see citing works
Self-citationHighly Conserved Protective Epitopes on Influenza B Viruses
Dreyfus, C., Laursen, N. S., Kwaks, T., Zuijdgeest, D., Khayat, R., Ekiert, D. C., Lee, J. H., Metlagel, Z., Bujny, M. V., Jongeneelen, M. A. C., et al. (2012) · Science · doi:10.1126/science.1222908 · Cited by 867 · see citing works
Augmented humoral and anaphylactic responses in FcγRII-deficient mice
Takai, T., Ono, M., Hikida, M., Ohmori, H., & Ravetch, J. V. (1996) · Nature · doi:10.1038/379346a0 · Cited by 826 · see citing works
Self-citationWrammert, J., Koutsonanos, D., Li, G., Edupuganti, S., Sui, J., Michael, M., McCausland, M. M., Skountzou, I., Hornig, M., Lipkin, W. I., et al. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20101352 · Cited by 777 · see citing works
FcγRIV: A Novel FcR with Distinct IgG Subclass Specificity
Nimmerjahn, F., Bruhns, P., Horiuchi, K., & Ravetch, J. V. (2005) · Immunity · doi:10.1016/j.immuni.2005.05.010 · Cited by 656 · see citing works
Self-citationImpaired IgG-Dependent Anaphylaxis and Arthus Reaction in FcγRIII (CD16) Deficient Mice
Hazenbos, W. L. W., Gessner, J. E., Hofhuis, F. M., Kuipers, H., Meyer, D., Heijnen, I., Schmidt, R. E., Sándor, M., Capel, P. J., Daëron, M., et al. (1996) · Immunity · doi:10.1016/s1074-7613(00)80494-x · Cited by 442 · see citing works
Couch, R. B., & Kasel, J. A. (1983) · Annual Review of Microbiology · doi:10.1146/annurev.mi.37.100183.002525 · Cited by 426 · see citing works
Jegerlehner, A., Schmitz, N., Storni, T., & Bachmann, M. F. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.9.5598 · Cited by 397 · see citing works
Li, G.-M., Chiu, C., Wrammert, J., McCausland, M. M., Andrews, S. F., Zheng, N., Lee, J.-H., Huang, M., Qu, X., Edupuganti, S., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118979109 · Cited by 393 · see citing works
The ferret as a model organism to study influenza A virus infection
Belser, J. A., Katz, J. M., & Tumpey, T. M. (2011) · Disease Models & Mechanisms · doi:10.1242/dmm.007823 · Cited by 364 · see citing works
Bakkouri, K. E., Descamps, F. J., Filette, M. D., Smet, A., Festjens, E., Birkett, A. J., van Rooijen, N., Verbeek, S. J., Fiers, W. C., & Saelens, X. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902147 · Cited by 335 · see citing works
Li, F., & Ravetch, J. V. (2011) · Science · doi:10.1126/science.1206954 · Cited by 331 · see citing works
Self-citationHuber, V. C., Lynch, J. M., Bucher, D. J., Le, J., & Metzger, D. W. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.12.7381 · Cited by 320 · see citing works
Ioan‐Facsinay, A., de Kimpe, S. J., Hellwig, S. M. M., van Lent, P. L., Hofhuis, F. M., van Ojik, H. H., Sedlik, C., da Silveira, S. A., Gerber, J. S., de Jong, Y. F., et al. (2002) · Immunity · doi:10.1016/s1074-7613(02)00294-7 · Cited by 304 · see citing works
Mouse model recapitulating human Fcγ receptor structural and functional diversity
Smith, P. T., DiLillo, D. J., Bournazos, S., Li, F., & Ravetch, J. V. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203954109 · Cited by 298 · see citing works
Self-citationWang, T. T., Tan, G. S., Hai, R., Pica, N., Petersen, E., Moran, T. M., & Palese, P. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000796 · Cited by 278 · see citing works
Self-citationNordstrom, J. L., Gorlatov, S. N., Zhang, W., Yang, Y., Huang, L., Burke, S., Li, H., Ciccarone, V. C., Zhāng, T., Stavenhagen, J. B., et al. (2011) · Breast Cancer Research · doi:10.1186/bcr3069 · Cited by 249 · see citing works
Antibodies, Fc receptors and cancer
Nimmerjahn, F., & Ravetch, J. V. (2007) · Current Opinion in Immunology · doi:10.1016/j.coi.2007.01.005 · Cited by 235 · see citing works
Self-citationAhmed, R., Oldstone, M. B. A., & Palese, P. (2007) · Nature Immunology · doi:10.1038/ni1530 · Cited by 227 · see citing works
Self-citationJegaskanda, S., Job, E. R., Kramski, M., Laurie, K., Isitman, G., Rose, R. D., Winnall, W. R., Stratov, I., Brööks, A. G., Reading, P. C., et al. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1201574 · Cited by 215 · see citing works
Manicassamy, B., Medina, R., Hai, R., Tsibane, T., Stertz, S., Nistal‐Villán, E., Palese, P., Basler, C. F., & García‐Sastre, A. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000745 · Cited by 197 · see citing works
Self-citationFcγRIV deletion reveals its central role for IgG2a and IgG2b activity in vivo
Nimmerjahn, F., Lux, A., Albert, H., Woigk, M., Lehmann, C. H. K., Dudziak, D., Smith, P. T., & Ravetch, J. V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014515107 · Cited by 195 · see citing works
Self-citationJegaskanda, S., Weinfurter, J. T., Friedrich, T. C., & Kent, S. J. (2013) · Journal of Virology · doi:10.1128/jvi.03030-12 · Cited by 184 · see citing works
A Pan-H1 Anti-Hemagglutinin Monoclonal Antibody with Potent Broad-Spectrum EfficacyIn Vivo
Tan, G. S., Krammer, F., Eggink, D., Kongchanagul, A., Moran, T. M., & Palese, P. (2012) · Journal of Virology · doi:10.1128/jvi.00469-12 · Cited by 161 · see citing works
Self-citationNimmerjahn, F., & Ravetch, J. V. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_86 · Cited by 154 · see citing works
Self-citationAn Antibody That Prevents the Hemagglutinin Low pH Fusogenic Transition
Barbey-Martin, C., Gigant, B., Bizebard, T., Calder, L. J., Wharton, S. A., Skehel, J. J., & Knossow, M. (2002) · Virology · doi:10.1006/viro.2001.1320 · Cited by 142 · see citing works
Mechanism of Neutralization of Influenza Virus Infectivity by Antibodies
Knossow, M., Gaudier, M., Douglas, A. R., Barrere, B., Bizebard, T., Barbey, C., Gigant, B., & Skehel, J. J. (2002) · Virology · doi:10.1006/viro.2002.1625 · Cited by 138 · see citing works
Torres, M., Fernaéndez-Fuentes, N., Fiser, A., & Casadevall, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700661200 · Cited by 132 · see citing works
Cetuximab-mediated Tumor Regression Depends on Innate and Adaptive Immune Responses
Yang, X., Zhang, X., Mortenson, E. D., Radkevich-Brown, O., Wang, Y., & Fu, Y. (2012) · Molecular Therapy · doi:10.1038/mt.2012.184 · Cited by 120 · see citing works
A requirement for FcγR in antibody-mediated bacterial toxin neutralization
Abboud, N., Chow, S.-K., Saylor, C., Markmann, A. J., Ravetch, J. V., Scharff, M. D., & Casadevall, A. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20100995 · Cited by 109 · see citing works
Self-citationSchlessinger, J., Steinberg, I. Z., Givol, D., Hochman, J., & Pecht, I. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.7.2775 · Cited by 107 · see citing works
Universal vaccine against influenza virus: Linking TLR signaling to anti‐viral protection
Schmitz, N., Beerli, R. R., Bauer, M., Jegerlehner, A., Dietmeier, K., Maudrich, M., Pumpens, P., Saudan, P., & Bachmann, M. F. (2012) · European Journal of Immunology · doi:10.1002/eji.201041225 · Cited by 84 · see citing works
Evidence of allosteric conformational changes in the antibody constant region upon antigen binding
Oda, M. (2003) · International Immunology · doi:10.1093/intimm/dxg036 · Cited by 79 · see citing works
Analyzing Antibody–Fc-Receptor Interactions
Nimmerjahn, F., & Ravetch, J. V. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-570-1_9 · Cited by 68 · see citing works
Self-citationHuman IgG Fc domain engineering enhances antitoxin neutralizing antibody activity
Bournazos, S., Chow, S.-K., Abboud, N., Casadevall, A., & Ravetch, J. V. (2014) · Journal of Clinical Investigation · doi:10.1172/jci72676 · Cited by 64 · see citing works
Self-citationTedder, T. F., Baras, A., & Xiu, Y. (2006) · Springer Seminars in Immunopathology · doi:10.1007/s00281-006-0057-9 · Cited by 61 · see citing works
Srivastava, V., Yang, Z., Hung, I. F., Xu, J., Zheng, B., & Zhang, Y. (2013) · Journal of Virology · doi:10.1128/jvi.00273-13 · Cited by 42 · see citing works
Neutralizing Anti-Influenza Virus Monoclonal Antibodies: Therapeutics and Tools for Discovery
Martinez, O., Tsibane, T., & Basler, C. F. (2009) · International Reviews of Immunology · doi:10.1080/08830180802593540 · Cited by 40 · see citing works
Tong, H., Zhang, L., Kaspar, A. A., Rames, M. J., Huang, L., Woodnutt, G., & Ren, G. (2013) · Scientific Reports · doi:10.1038/srep01089 · Cited by 34 · see citing works
Barkas, T. P., & Watson, C. M. (1979) · PubMed · Cited by 28 · see citing works
Wang, T. T., & Palese, P. (2011) · Science · doi:10.1126/science.1210724 · Cited by 24 · see citing works
Self-citationReale, M. A., Manheimer-Lory, A., Moran, T. M., Norton, G., Bona, C., & Schulman, J. L. (1986) · The Journal of Immunology · doi:10.4049/jimmunol.137.4.1352 · Cited by 21 · see citing works
Non‐covalent interactions between Fab and Fc regions in immunoglobulin G molecules
Kilár, F., & Závodszky, P. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb10541.x · Cited by 12 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395 · see citing works
Beyond binding: antibody effector functions in infectious diseases
Lu, L. L., Suscovich, T. J., Fortune, S. M., & Alter, G. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.106 · Cited by 810 · see citing works
The human antibody response to influenza A virus infection and vaccination
Krammer, F. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0143-6 · Cited by 805 · see citing works
Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection
Yassine, H. M., Boyington, J. C., McTamney, P. M., Wei, C., Kanekiyo, M., Kong, W., Gallagher, J. R., Wang, L., Zhang, Y., Joyce, M. G., et al. (2015) · Nature Medicine · doi:10.1038/nm.3927 · Cited by 702 · see citing works
Antibody Structure and Function: The Basis for Engineering Therapeutics
Chiu, M. L., Goulet, D. R., Teplyakov, A., & Gilliland, G. L. (2019) · Antibodies · doi:10.3390/antib8040055 · Cited by 646 · see citing works
The role of IgG Fc receptors in antibody-dependent enhancement
Bournazos, S., Gupta, A., & Ravetch, J. V. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-00410-0 · Cited by 619 · see citing works
Self-citationA stable trimeric influenza hemagglutinin stem as a broadly protective immunogen
Impagliazzo, A., Milder, F. J., Kuipers, H., Wagner, M. V., Zhu, X., Hoffman, R. M. B., van Meersbergen, R., Huizingh, J., Wanningen, P., Verspuij, J. W. A., et al. (2015) · Science · doi:10.1126/science.aac7263 · Cited by 591 · see citing works
Advances in the development of influenza virus vaccines
Krammer, F., & Palese, P. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4529 · Cited by 592 · see citing works
Self-citationMouse and human FcR effector functions
Bruhns, P., & Jönsson, F. (2015) · Immunological Reviews · doi:10.1111/imr.12350 · Cited by 573 · see citing works
A Functional Role for Antibodies in Tuberculosis
Lu, L. L., Chung, A. W., Rosebrock, T. R., Ghebremichael, M. S., Yu, W., Grace, P. S., Schoen, M. K., Tafesse, F., Martin, C. J., Leung, V. W. Y., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.072 · Cited by 560 · see citing works
Immunological mechanisms of vaccine-induced protection against COVID-19 in humans
Sadarangani, M., Marchant, A., & Kollmann, T. R. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00578-z · Cited by 560 · see citing works
Type I and type II Fc receptors regulate innate and adaptive immunity
Pincetic, A., Bournazos, S., DiLillo, D. J., Maamary, J., Wang, T. T., Dahan, R., Fiebiger, B. M., & Ravetch, J. V. (2014) · Nature Immunology · doi:10.1038/ni.2939 · Cited by 504 · see citing works
Self-citationBroadly Neutralizing Anti-HIV-1 Antibodies Require Fc Effector Functions for In Vivo Activity
Bournazos, S., Klein, F., Pietzsch, J., Seaman, M. S., Nussenzweig, M. C., & Ravetch, J. V. (2014) · Cell · doi:10.1016/j.cell.2014.08.023 · Cited by 493 · see citing works
Self-citationA perspective on potential antibody-dependent enhancement of SARS-CoV-2
Arvin, A. M., Fink, K., Schmid, M. A., Cathcart, A., Spreafico, R., Havenar-Daughton, C., Lanzavecchia, A., Corti, D., & Virgin, H. W. (2020) · Nature · doi:10.1038/s41586-020-2538-8 · Cited by 485 · see citing works
Activity of convalescent and vaccine serum against SARS-CoV-2 Omicron
Carreño, J. M., Alshammary, H., Tcheou, J., Singh, G., Raskin, A. J., Kawabata, H., Sominsky, L. A., Clark, J. J., Adelsberg, D. C., Bielak, D. A., et al. (2021) · Nature · doi:10.1038/s41586-022-04399-5 · Cited by 456 · see citing works
Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes
Kallewaard, N. L., Corti, D., Collins, P. J., Neu, U., McAuliffe, J. M., Benjamin, E., Wachter-Rosati, L., Palmer‐Hill, F. J., Yuan, A. Q., Walker, P. A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.073 · Cited by 410 · see citing works
Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection
DiLillo, D. J., Palese, P., Wilson, P. C., & Ravetch, J. V. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84428 · Cited by 409 · see citing works
Self-citationBroad betacoronavirus neutralization by a stem helix–specific human antibody
Pinto, D., Sauer, M. M., Czudnochowski, N., Low, J. S., Tortorici, M. A., Housley, M. P., Noack, J., Walls, A. C., Bowen, J. E., Guarino, B., et al. (2021) · Science · doi:10.1126/science.abj3321 · Cited by 381 · see citing works
Tackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.05.005 · Cited by 375 · see citing works
Winkler, E. S., Gilchuk, P., Yu, J., Bailey, A. L., Chen, R. E., Chong, Z., Zost, S. J., Jang, H., Huang, Y., Allen, J. D., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.026 · Cited by 366 · see citing works
Suryadevara, N., Shrihari, S., Gilchuk, P., VanBlargan, L. A., Binshtein, E., Zost, S. J., Nargi, R. S., Sutton, R. E., Winkler, E. S., Chen, E. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.029 · Cited by 397 · see citing works
A multivalent nucleoside-modified mRNA vaccine against all known influenza virus subtypes
Arevalo, C. P., Bolton, M. J., Sage, V. L., Ye, N., Furey, C., Muramatsu, H., Alameh, M., Pardi, N., Drapeau, E. M., Parkhouse, K., et al. (2022) · Science · doi:10.1126/science.abm0271 · Cited by 358 · see citing works
Dissecting polyclonal vaccine-induced humoral immunity against HIV using Systems Serology
Chung, A., Kumar, M. P., Arnold, K. B., Yu, W.-H., Schoen, M., Dunphy, L. J., Suscovich, T., Frahm, N., Linde, C., Mahan, A. E., et al. (2015) · Cell · doi:10.1016/j.cell.2015.10.027 · Cited by 360 · see citing works
Nachbagauer, R., Feser, J., Naficy, A. B., Bernstein, D. I., Guptill, J. T., Walter, E. B., Berlanda-Scorza, F., Stadlbauer, D., Wilson, P. C., Aydillo, T., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-1118-7 · Cited by 340 · see citing works
Self-citationModulating IgG effector function by Fc glycan engineering
Li, T., DiLillo, D. J., Bournazos, S., Giddens, J. P., Ravetch, J. V., & Wang, L. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702173114 · Cited by 316 · see citing works
Self-citationBarrett, J. R., Belij-Rammerstorfer, S., Dold, C., Ewer, K. J., Folegatti, P. M., Gilbride, C., Halkerston, R., Hill, J., Jenkin, D., Stockdale, L., et al. (2021) · Nature Medicine · doi:10.1038/s41591-020-01179-4 · Cited by 315 · see citing works
Schäfer, A., Muecksch, F., Lorenzi, J. C. C., Leist, S. R., Cipolla, M., Bournazos, S., Schmidt, F., Maison, R. M., Gazumyan, A., Martinez, D. R., et al. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20201993 · Cited by 305 · see citing works
Self-citationIntegrative Physiology of Pneumonia
Quinton, L. J., Walkey, A. J., & Mizgerd, J. P. (2018) · Physiological Reviews · doi:10.1152/physrev.00032.2017 · Cited by 308 · see citing works
NAction! How Can Neuraminidase-Based Immunity Contribute to Better Influenza Virus Vaccines?
Krammer, F., Fouchier, R. A. M., Eichelberger, M. C., Webby, R. J., Shaw‐Saliba, K., Wan, H., Wilson, P. C., Compans, R. W., Skountzou, I., & Monto, A. S. (2018) · mBio · doi:10.1128/mbio.02332-17 · Cited by 291 · see citing works
Irani, V., Guy, A. J., Andrew, D. W., Beeson, J. G., Ramsland, P. A., & Richards, J. S. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.03.255 · Cited by 290 · see citing works
Pardi, N., Parkhouse, K., Kirkpatrick, E., McMahon, M., Zost, S. J., Mui, B. L., Tam, Y. K., Karikó, K., Barbosa, C. J., Madden, T. D., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05482-0 · Cited by 281 · see citing works
Fc-Mediated Antibody Effector Functions During Respiratory Syncytial Virus Infection and Disease
van Erp, E. A., Luytjes, W., Ferwerda, G., & van Kasteren, P. B. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00548 · Cited by 281 · see citing works
Lee, J., Boutz, D. R., Chromikova, V., Joyce, M. G., Vollmers, C., Leung, K., Horton, A. P., DeKosky, B. J., Lee, C., Lavinder, J. J., et al. (2016) · Nature Medicine · doi:10.1038/nm.4224 · Cited by 278 · see citing works
SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2
Amanat, F., Thapa, M., Lei, T., Ahmed, S. M. S., Adelsberg, D. C., Carreño, J. M., Strohmeier, S., Schmitz, A. J., Zafar, S., Zhou, J. Q., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.005 · Cited by 273 · see citing works
Mucosal immune responses to infection and vaccination in the respiratory tract
Mettelman, R. C., Allen, E. K., & Thomas, P. G. (2022) · Immunity · doi:10.1016/j.immuni.2022.04.013 · Cited by 272 · see citing works
Henry Dunand, C. J., Leon, P. E., Huang, M., Choi, A., Chromikova, V., Ho, I. Y., Tan, G. S., Cruz, J., Hirsh, A., Zheng, N.-Y., et al. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.05.014 · Cited by 268 · see citing works
Self-citationDifferential Fc-Receptor Engagement Drives an Anti-tumor Vaccinal Effect
DiLillo, D. J., & Ravetch, J. V. (2015) · Cell · doi:10.1016/j.cell.2015.04.016 · Cited by 262 · see citing works
Self-citationIrrgang, P., Gerling, J., Kocher, K., Lapuente, D., Steininger, P. A., Habenicht, K. M., Wytopil, M., Beileke, S., Schäfer, S., Zhong, J., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.ade2798 · Cited by 259 · see citing works
Broadly protective human antibodies that target the active site of influenza virus neuraminidase
Stadlbauer, D., Zhu, X., McMahon, M., Turner, J. S., Wohlbold, T. J., Schmitz, A. J., Strohmeier, S., Yu, W., Nachbagauer, R., Mudd, P. A., et al. (2019) · Science · doi:10.1126/science.aay0678 · Cited by 261 · see citing works
A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface
Bangaru, S., Lang, S., Schotsaert, M., Vanderven, H. A., Zhu, X., Kose, N., Bombardi, R. G., Finn, J. A., Kent, S. J., Gilchuk, P., et al. (2019) · Cell · doi:10.1016/j.cell.2019.04.011 · Cited by 246 · see citing works
Antibody-Dependent Cellular Phagocytosis in Antiviral Immune Responses
Tay, M. Z., Wiehe, K. J., & Pollara, J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00332 · Cited by 229 · see citing works
Signaling by Antibodies: Recent Progress
Bournazos, S., Wang, T. T., Dahan, R., Maamary, J., & Ravetch, J. V. (2017) · Annual Review of Immunology · doi:10.1146/annurev-immunol-051116-052433 · Cited by 230 · see citing works
Self-citationAptamer Blocking Strategy Inhibits SARS‐CoV‐2 Virus Infection
Sun, M., Liu, S., Wei, X., Wan, S., Huang, M., Song, T., Lu, Y. W. W., Weng, X., Zhu, L., Chen, H., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202100225 · Cited by 228 · see citing works
Neutralization of Virus Infectivity by Antibodies: Old Problems in New Perspectives
Klasse, P. J. (2014) · Advances in Biology · doi:10.1155/2014/157895 · Cited by 227 · see citing works
Cathcart, A. L., Havenar‐Daughton, C., Lempp, F. A., Ma, D., Schmid, M., Agostini, M. L., Guarino, B., di Iulio, J., Rosen, L. E., Tucker, H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.09.434607 · Cited by 206 · see citing works
Laursen, N. S., Friesen, R. H. E., Zhu, X., Jongeneelen, M. A. C., Blokland, S., Vermond, J., Real, A. V. E.-O., Tang, C., van Diepen, H. A., Obmolova, G., et al. (2018) · Science · doi:10.1126/science.aaq0620 · Cited by 223 · see citing works
Influenza Hemagglutinin and Neuraminidase: Yin–Yang Proteins Coevolving to Thwart Immunity
Košík, I., & Yewdell, J. W. (2019) · Viruses · doi:10.3390/v11040346 · Cited by 223 · see citing works
Beyond neutralization: Fc-dependent antibody effector functions in SARS-CoV-2 infection
Zhang, A., Stacey, H. D., D’Agostino, M. R., Tugg, Y., Marzok, A., & Miller, M. S. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00813-1 · Cited by 212 · see citing works
Ullah, I., Prévost, J., Ladinsky, M., Stone, H., Lu, M.-L., Anand, S., Beaudoin-Bussières, G., Symmes, K., Benlarbi, M., Ding, S.-L., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.015 · Cited by 152 · see citing works
Johnson, J. L., Rosenthal, R. L., Knox, J. J., Myles, A., Naradikian, M. S., Madej, J., Kostiv, M., Rosenfeld, A. M., Meng, W., Christensen, S. R., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.03.020 · Cited by 212 · see citing works
Extremely potent human monoclonal antibodies from COVID-19 convalescent patients
Andreano, E., Nicastri, E., Paciello, I., Pileri, P., Manganaro, N., Piccini, G., Manenti, A., Pantano, E., Kabanova, A., Troisi, M., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.035 · Cited by 198 · see citing works
Current and future influenza vaccines
Yamayoshi, S., & Kawaoka, Y. (2019) · Nature Medicine · doi:10.1038/s41591-018-0340-z · Cited by 203 · see citing works
Novel correlates of protection against pandemic H1N1 influenza A virus infection
Ng, S., Nachbagauer, R., Balmaseda, Á., Stadlbauer, D., Ojeda, S., PATEL, M. J., Rajabhathor, A., López, R., Guglia, A. F., Sánchez, N., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0463-x · Cited by 201 · see citing works
A common glycan structure on immunoglobulin G for enhancement of effector functions
Lin, C., Tsai, M.-H., Li, S., Tsai, T.-I., Chu, K., Liu, Y.-C., Lai, M.-Y., Wu, C.-Y., Tseng, Y.-C., Shivatare, S. S., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1513456112 · Cited by 200 · see citing works
Multiplexed Fc array for evaluation of antigen-specific antibody effector profiles
Brown, E. P., Dowell, K. G., Boesch, A. W., Normandin, E., Mahan, A. E., Chu, T. H., Barouch, D. H., Bailey‐Kellogg, C., Alter, G., & Ackerman, M. E. (2017) · Journal of Immunological Methods · doi:10.1016/j.jim.2017.01.010 · Cited by 197 · see citing works
Functional diversification of IgGs through Fc glycosylation
Wang, T. T., & Ravetch, J. V. (2019) · Journal of Clinical Investigation · doi:10.1172/jci130029 · Cited by 193 · see citing works
Self-citationAnimal models for influenza virus pathogenesis, transmission, and immunology
Thangavel, R. R., & Bouvier, N. M. (2014) · Journal of Immunological Methods · doi:10.1016/j.jim.2014.03.023 · Cited by 185 · see citing works
Double-layered protein nanoparticles induce broad protection against divergent influenza A viruses
Deng, L., Mohan, T., Chang, T. Z., Gonzalez, G. X., Wang, Y., Kwon, Y., Kang, S., Compans, R. W., Champion, J. A., & Wang, B. (2018) · Nature Communications · doi:10.1038/s41467-017-02725-4 · Cited by 190 · see citing works
Watanabe, A., McCarthy, K. R., Kuraoka, M., Schmidt, A. G., Adachi, Y., Onodera, T., Tonouchi, K., Caradonna, T. M., Bajic, G., Song, S., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.048 · Cited by 190 · see citing works
Fc-engineered antibody therapeutics with improved anti-SARS-CoV-2 efficacy
Yamin, R., Jones, A., Hoffmann, H.-H., Schäfer, A., Kao, K. S., Francis, R., Sheahan, T. P., Baric, R. S., Rice, C. M., Ravetch, J. V., et al. (2021) · Nature · doi:10.1038/s41586-021-04017-w · Cited by 187 · see citing works
Self-citationUniversal influenza virus vaccines and therapeutic antibodies
Nachbagauer, R., & Krammer, F. (2017) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2017.02.009 · Cited by 184 · see citing works
Carter, D. M., Darby, C. A., Lefoley, B. C., Crevar, C. J., Alefantis, T. G., Oomen, R. P., Anderson, S. F., Strugnell, T., Cortés-Garcia, G., Vogel, T. U., et al. (2016) · Journal of Virology · doi:10.1128/jvi.03152-15 · Cited by 182 · see citing works
He, W., Tan, G. S., Mullarkey, C. E., Lee, A. J., Lam, M. M. W., Krammer, F., Henry, C., Wilson, P. C., Ashkar, A. A., Palese, P., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1609316113 · Cited by 180 · see citing works
Self-citationWu, N. C., & Wilson, I. A. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.06.015 · Cited by 176 · see citing works
FcγR dependent mechanisms of cytotoxic, agonistic, and neutralizing antibody activities
Nimmerjahn, F., Gordan, S., & Lux, A. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.04.005 · Cited by 171 · see citing works
Viral Receptor-Binding Site Antibodies with Diverse Germline Origins
Schmidt, A. G., Therkelsen, M. D., Stewart, S. M., Kepler, T. B., Liao, H., Moody, M. A., Haynes, B. F., & Harrison, S. C. (2015) · Cell · doi:10.1016/j.cell.2015.04.028 · Cited by 172 · see citing works
Defining the antibody cross-reactome directed against the influenza virus surface glycoproteins
Nachbagauer, R., Choi, A., Hirsh, A., Margine, I., Iida, S., Barrera, A., Marcela Ferrés, G., Albrecht, R. A., García‐Sastre, A., Bouvier, N. M., et al. (2017) · Nature Immunology · doi:10.1038/ni.3684 · Cited by 172 · see citing works
Self-citationDefining the risk of SARS-CoV-2 variants on immune protection
DeGrace, M. M., Ghedin, E., Frieman, M. B., Krammer, F., Grifoni, A., Alisoltani, A., Alter, G., Amara, R. R., Baric, R. S., Barouch, D. H., et al. (2022) · Nature · doi:10.1038/s41586-022-04690-5 · Cited by 167 · see citing works
Antiviral Approaches against Influenza Virus
Kumari, R., Sharma, S. D., Kumar, A., Ende, Z. S., Mishina, M., Wang, Y., Falls, Z., Samudrala, R., Pohl, J., Knight, P. R., et al. (2023) · Clinical Microbiology Reviews · doi:10.1128/cmr.00040-22 · Cited by 172 · see citing works
He, W., Chen, C.-J., Mullarkey, C. E., Hamilton, J. R., Wong, C. K., Leon, P. E., Uccellini, M. B., Chromikova, V., Henry, C., Hoffman, K. W., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00928-3 · Cited by 166 · see citing works
Self-citationM2e-Based Universal Influenza A Vaccines
Deng, L., Cho, K., Fiers, W. C., & Saelens, X. (2015) · Vaccines · doi:10.3390/vaccines3010105 · Cited by 168 · see citing works
Houser, K. V., Chen, G. L., Carter, C., Crank, M. C., Nguyen, T., Florez, M. C. B., Berkowitz, N. M., Mendoza, F. H., Hendel, C. S., Gordon, I. J., et al. (2022) · Nature Medicine · doi:10.1038/s41591-021-01660-8 · Cited by 165 · see citing works
Self-citationSize-Dependent Segregation Controls Macrophage Phagocytosis of Antibody-Opsonized Targets
Bakalar, M. H., Joffe, A. M., Schmid, E. M., Son, S., Podolski, M., & Fletcher, D. A. (2018) · Cell · doi:10.1016/j.cell.2018.05.059 · Cited by 153 · see citing works
Is a Universal Influenza Virus Vaccine Possible?
Nachbagauer, R., & Palese, P. (2019) · Annual Review of Medicine · doi:10.1146/annurev-med-120617-041310 · Cited by 159 · see citing works
Self-citationDoud, M. B., Lee, J. M., & Bloom, J. D. (2018) · Nature Communications · doi:10.1038/s41467-018-03665-3 · Cited by 158 · see citing works
The role of Fc–FcγR interactions in IgG-mediated microbial neutralization
Bournazos, S., DiLillo, D. J., & Ravetch, J. V. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20151267 · Cited by 154 · see citing works
Self-citationA versatile high-throughput assay to characterize antibody-mediated neutrophil phagocytosis
Karsten, C. B., Mehta, N., Shin, S. A., Diefenbach, T. J., Slein, M. D., Karpinski, W., Irvine, E. B., Broge, T. A., Suscovich, T. J., & Alter, G. (2019) · Journal of Immunological Methods · doi:10.1016/j.jim.2019.05.006 · Cited by 154 · see citing works
Antiviral neutralizing antibodies: from in vitro to in vivo activity
Burton, D. R. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00858-w · Cited by 152 · see citing works
Wu, Y., Cho, M., Shore, D. A., Song, M., Choi, J.-A., Jiang, T., Deng, Y., Bourgeois, M. A., Almli, L. M., Yang, H., et al. (2015) · Nature Communications · doi:10.1038/ncomms8708 · Cited by 150 · see citing works
Case, J. B., Mackin, S., Errico, J. M., Chong, Z., Madden, E. A., Whitener, B. M., Guarino, B., Schmid, M., Rosenthal, K., Ren, K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31615-7 · Cited by 144 · see citing works
Nachbagauer, R., Choi, A., Izikson, R., Cox, M. M. J., Palese, P., & Krammer, F. (2016) · mBio · doi:10.1128/mbio.01996-15 · Cited by 149 · see citing works
Self-citationTRIM21—From Intracellular Immunity to Therapy
Foss, S., Bottermann, M., Jonsson, A., Sandlie, I., James, L. C., & Andersen, J. T. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02049 · Cited by 146 · see citing works
Fcγ receptor pathways during active and passive immunization
Bournazos, S., & Ravetch, J. V. (2015) · Immunological Reviews · doi:10.1111/imr.12343 · Cited by 147 · see citing works
Self-citationTan, G. S., Leon, P. E., Albrecht, R. A., Margine, I., Hirsh, A., Bahl, J., & Krammer, F. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005578 · Cited by 147 · see citing works
Self-citationConserved epitope on influenza-virus hemagglutinin head defined by a vaccine-induced antibody
Raymond, D. D., Bajic, G., Ferdman, J., Suphaphiphat, P., Settembre, E. C., Moody, M. A., Schmidt, A. G., & Harrison, S. C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715471115 · Cited by 145 · see citing works
Engineered mRNA-expressed antibodies prevent respiratory syncytial virus infection
Tiwari, P. M., Vanover, D. A., Lindsay, K. E., Bawage, S. S., Kirschman, J. L., Bhosle, S. M., Lifland, A. W., Zurla, C., & Santangelo, P. J. (2018) · Nature Communications · doi:10.1038/s41467-018-06508-3 · Cited by 139 · see citing works
Fc-optimized antibodies elicit CD8 immunity to viral respiratory infection
Bournazos, S., Corti, D., Virgin, H. W., & Ravetch, J. V. (2020) · Nature · doi:10.1038/s41586-020-2838-z · Cited by 139 · see citing works
Self-citationThe role and function of Fcγ receptors on myeloid cells
Bournazos, S., Wang, T. T., & Ravetch, J. V. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.mchd-0045-2016 · Cited by 138 · see citing works
Self-citationInactivated influenza vaccines
Fiore, A. E., Bridges, C. B., Katz, J. M., & Cox, N. J. (2013) · Elsevier eBooks · doi:10.1016/b978-1-4557-0090-5.00026-4 · Cited by 135 · see citing works
DiLillo, D. J., & Ravetch, J. V. (2015) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-15-0120 · Cited by 132 · see citing works
Self-citationTackling influenza with broadly neutralizing antibodies
Corti, D., Cameroni, E., Guarino, B., Kallewaard, N. L., Zhu, Q., & Lanzavecchia, A. (2017) · Current Opinion in Virology · doi:10.1016/j.coviro.2017.03.002 · Cited by 133 · see citing works
Lindgren, G., Ols, S., Liang, F., Thompson, E. A., Lin, A., Hellgren, F., Bahl, K., John, S., Yuzhakov, O., Hassett, K. J., et al. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01539 · Cited by 132 · see citing works
Tay, M. Z., Liu, P., Williams, L. D., McRaven, M. D., Sawant, S. S., Gurley, T. C., Xu, T. T., Dennison, S. M., Liao, H., Chenine, A., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005817 · Cited by 131 · see citing works
Wohlbold, T. J., Podolsky, K. A., Chromikova, V., Roubidoux, E. K., Falconieri, V., Meade, P. S., Amanat, F., Tan, J., tenOever, B. R., Tan, G. S., et al. (2017) · Nature Microbiology · doi:10.1038/s41564-017-0011-8 · Cited by 130 · see citing works
Self-citationZhang, T., Yuan, Q., Zhao, J.-H., Zhang, Y., Yuan, L., Lan, Y., Lo, Y.-C., Sun, C., Wu, C., Zhang, J., et al. (2015) · Gut · doi:10.1136/gutjnl-2014-308964 · Cited by 126 · see citing works
Antibody Immunodominance: The Key to Understanding Influenza Virus Antigenic Drift
Altman, M. O., Angeletti, D., & Yewdell, J. W. (2018) · Viral Immunology · doi:10.1089/vim.2017.0129 · Cited by 127 · see citing works
Antiviral Monoclonal Antibodies: Can They Be More Than Simple Neutralizing Agents?
Pelegrín, M., Naranjo‐Gómez, M., & Piechaczyk, M. (2015) · Trends in Microbiology · doi:10.1016/j.tim.2015.07.005 · Cited by 123 · see citing works
Stalking influenza by vaccination with pre-fusion headless HA mini-stem
Valkenburg, S. A., Mallajosyula, V. V. A., Li, O. T. W., Chin, A. W. H., Carnell, G., Temperton, N. J., Varadarajan, R., & Poon, L. L. M. (2016) · Scientific Reports · doi:10.1038/srep22666 · Cited by 123 · see citing works
A potent human neutralizing antibody Fc-dependently reduces established HBV infections
Li, D., He, W., Liu, X., Zheng, S., Qi, Y., Li, H., Mao, F., Liu, J., Sun, Y., Pan, L., et al. (2017) · eLife · doi:10.7554/elife.26738 · Cited by 122 · see citing works
The Multifaceted B Cell Response to Influenza Virus
Lam, J. H., & Baumgarth, N. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1801208 · Cited by 119 · see citing works
- Authors
- DiLillo, D. J., Tan, G. S., Palese, P., & Ravetch, J. V.
- Affiliations
- Rockefeller University (US)
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Ravetch, Jeffrey V
- Venue
- Nature Medicine
- Published
- 2014-01-12
- Volume
- 20
- Issue
- 2
- Pages
- 143-151
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- PMC
- PMC3966466
- OpenAlex
- W2161738112
- Cited by
- 749
- References
- 53
- Citations by year
- 2026: 38 · 2025: 44 · 2024: 32 · 2023: 58 · 2022: 59 · 2021: 77 · 2020: 52 · 2019: 86 · 2018: 68 · 2017: 74 · 2016: 64 · 2015: 62 · 2014: 32 · 2013: 1 · 2012: 1
- FWCI
- 54.50
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Bill and Melinda Gates Foundation
- Leukemia and Lymphoma Society
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (U19AI109946, HHSN266200700010C, P01AI097092, R01AI035875, AI097092, P01AI081677, U54AI057158)
- Army Research Office
- Army Research Laboratory
- Topics
- Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Keywords
- influenza virus, hemagglutinin stalk, broadly neutralizing antibodies, Fc gamma receptor, antibody-dependent cellular cytotoxicity, antibody-mediated protection, immune complexes, H1N1 influenza, antibody engineering, neutralizing monoclonal antibodies
- MeSH terms
- Animals, Antibodies, Monoclonal, Antigen-Antibody Complex, Cell Line, Chick Embryo, Dogs, Enzyme-Linked Immunosorbent Assay, Humans, Killer Cells, Natural, Mice, Inbred C57BL, Neutralization Tests, Receptors, IgG, Mice, Knockout, Hemagglutinin Glycoproteins, Influenza Virus, Surface Plasmon Resonance, Mice, Influenza A Virus, H1N1 Subtype, Kaplan-Meier Estimate, Antibodies, Neutralizing
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
