Antimicrobial proteins: from old proteins, new tricks

Smith, Valerie J.; Dyrynda, Elisabeth A.

doi:10.1016/j.molimm.2015.08.009

Cited by 85Antimicrobial Peptides and ActivitiesInvertebrate Immune Response MechanismsAquaculture disease management and microbiota

Antimicrobial proteins: from old proteins, new tricks

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Smith, Valerie J., Dyrynda, Elisabeth A.·2015·Molecular Immunology

DOI 10.1016/j.molimm.2015.08.009

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Abstract

This review describes the main types of antimicrobial peptides (AMPs) synthesised by crustaceans, primarily those identified in shrimp, crayfish, crab and lobster. It includes an overview of their range of microbicidal activities and the current landscape of our understanding of their gene expression patterns in different body tissues. It further summarises how their expression might change following various types of immune challenges. The review further considers proteins or protein fragments from crustaceans that have antimicrobial properties but are more usually associated with other biological functions, or are derived from such proteins. It discusses how these unconventional AMPs might be generated at, or delivered to, sites of infection and how they might contribute to crustacean host defence in vivo. It also highlights recent work that is starting to reveal the extent of multi-functionality displayed by some decapod AMPs, particularly their participation in other aspects of host protection. Examples of such activities include proteinase inhibition, phagocytosis, antiviral activity and haematopoiesis.

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Molecular characterization of three crustin genes in the morotoge shrimp, Pandalopsis japonica
Kim, M., Jeon, J.-M., Oh, C., Kim, Y. M., Lee, D. S., Kang, C.-K., & Kim, H.-W. (2012) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2012.05.007 · Cited by 20 · see citing works
Profiling of a few immune responsive genes expressed in postlarvae of Fenneropenaeus indicus challenged with Vibrio harveyi D3
Nayak, S., Ajay, K. M., Ramaiah, N., Meena, R. M., & Sreepada, R. A. (2011) · Journal of Invertebrate Pathology · doi:10.1016/j.jip.2011.04.001 · Cited by 19 · see citing works
cDNA cloning, characterization and expression analysis of a novel antimicrobial peptide gene penaeidin-3 (Fi-Pen3) from the haemocytes of Indian white shrimp Fenneropenaeus indicus
Shanthi, S. A., & Vaseeharan, B. (2011) · Microbiological Research · doi:10.1016/j.micres.2011.07.003 · Cited by 18 · see citing works
Immunology of Invertebrates: Cellular
Smith, V. J. (2010) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0002344.pub2 · Cited by 18 · see citing works
Self-citation
Survivability of Penaeus monodon during white spot syndrome virus infection and its correlation with immune related genes
Jeswin, J., Anju, A., Thomas, P. C., Paulton, M. P., & Vijayan, K. K. (2012) · Aquaculture · doi:10.1016/j.aquaculture.2012.12.004 · Cited by 16 · see citing works
Immune responses of whiteleg shrimp, L itopenaeus vannamei ( B oone, 1931), to bacterially expressed ds RNA specific to VP 28 gene of white spot syndrome virus
Taju, G., Madan, N., Majeed, S. A., Kumar, T. R., Thamizhvanan, S., Otta, S. K., & Hameed, A. S. S. (2014) · Journal of Fish Diseases · doi:10.1111/jfd.12256 · Cited by 16 · see citing works
Flightless-I (FliI) is a potential negative regulator of the Toll pathway in Litopenaeus vannamei
Zhang, S., Qiu, W., Chen, Y.-G., Yuan, F.-H., Li, C., Yan, H., Weng, S., & He, J. (2014) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2014.10.023 · Cited by 15 · see citing works
Molecular cloning and characterization of three novel Hemocyanins from Chinese mitten crab, Eriocheir sinensis
Huang, Y. K., Huang, X. H., Hou, L., An, L., Hui, K.-M., Ren, Q., & Wang, W. (2014) · Aquaculture · doi:10.1016/j.aquaculture.2014.07.033 · Cited by 14 · see citing works
Yellow head virus binding to cell surface proteins from Penaeus monodon hemocytes
Havanapan, P., Taengchaiyaphum, S., Bourchookarn, A., Ketterman, A. J., & Krittanai, C. (2014) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2014.08.014 · Cited by 8 · see citing works
Effects of Dietary β‐1,3‐Glucan on Expression of Immune‐related Genes of Litopenaeus vannamei Exposed to Nitrite‐N
Zhao, H., Cao, J., Wang, A., Huang, Y. H., Li, G., & Lan, H. (2012) · Journal of the World Aquaculture Society · doi:10.1111/j.1749-7345.2012.00568.x · Cited by 6 · see citing works
The shrimp immune system
Smith, V. J., Roulston, C., & Dyrynda, E. A. (2012) · Nottingham University Press eBooks · doi:10.7313/upo9781907284939.006 · Cited by 6 · see citing works
Self-citation
cDNA CLONING, CHARACTERIZATION AND mRNA EXPRESSION OF A HYASTATIN-LIKE GENE FROM SWIMMING CRAB PORTUNUS TRITUBERCULATUS
Ri, W. (2010) · Haiyang yu huzhao · Cited by 1 · see citing works

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Designing improved active peptides for therapeutic approaches against infectious diseases
Gomes, B., Augusto, M. T., Felício, M. R., Hollmann, A., Franco, O. L., Gonçalves, S., & Santos, N. C. (2018) · Biotechnology Advances · doi:10.1016/j.biotechadv.2018.01.004 · Cited by 173 · see citing works
Antimicrobial peptides in marine invertebrate health and disease
Destoumieux-Garzón, D., Rosa, R. D., Schmitt, P., Barreto, C., Vidal-Dupiol, J., Mitta, G., Gueguen, Y., & Bachère, E. (2016) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2015.0300 · Cited by 160 · see citing works
Clinical Applications of Antimicrobial Peptides (AMPs): Where do we Stand Now?
Divyashree, M., Mani, M. K., Reddy, D., Kumavath, R., Ghosh, P., Azevedo, V., & Barh, D. (2019) · Protein and Peptide Letters · doi:10.2174/0929866526666190925152957 · Cited by 146 · see citing works
The COVID-19 pandemic: Important considerations for contact lens practitioners
Jones, L., Walsh, K., Willcox, M. D. P., Morgan, P. B., & Nichols, J. J. (2020) · Contact Lens and Anterior Eye · doi:10.1016/j.clae.2020.03.012 · Cited by 122 · see citing works
The stress–immunity axis in shellfish
Coates, C. J., & Söderhäll, K. (2020) · Journal of Invertebrate Pathology · doi:10.1016/j.jip.2020.107492 · Cited by 89 · see citing works
On the silver jubilee of crustacean antimicrobial peptides
Matos, G. M., & Rosa, R. D. (2021) · Reviews in Aquaculture · doi:10.1111/raq.12614 · Cited by 73 · see citing works
Marine Invertebrate Antimicrobial Peptides and Their Potential as Novel Peptide Antibiotics
Guryanova, S., Balandin, S. V., Belogurova-Ovchinnikova, O., & Ovchinnikova, T. (2023) · Marine Drugs · doi:10.3390/md21100503 · Cited by 53 · see citing works
Hemolymph proteins: An overview across marine arthropods and molluscs
Gianazza, E., Eberini, I., Palazzolo, L., & Miller, I. (2021) · Journal of Proteomics · doi:10.1016/j.jprot.2021.104294 · Cited by 61 · see citing works
The New Antimicrobial Peptide SpHyastatin from the Mud Crab Scylla paramamosain with Multiple Antimicrobial Mechanisms and High Effect on Bacterial Infection
Shan, Z., Zhu, K., Peng, H., Chen, B., Liu, J., Chen, F., Ma, X., Wang, S., Qiao, K., & Wang, K. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01140 · Cited by 61 · see citing works
Immunology of Invertebrates: Cellular
Smith, V. J. (2016) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0002344.pub3 · Cited by 57 · see citing works
Self-citation
The expanding repertoire of immune‐related molecules with antimicrobial activity in penaeid shrimps: a review
Aweya, J. J., Zheng, Z., Zheng, X., Yao, D., & Zhang, Y. (2021) · Reviews in Aquaculture · doi:10.1111/raq.12551 · Cited by 51 · see citing works
The Immune System of Crustaceans
Rowley, A. F. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-374279-7.12005-3 · Cited by 51 · see citing works
SpToll1 and SpToll2 modulate the expression of antimicrobial peptides in Scylla paramamosain
Chen, Y., Aweya, J., Sun, W.-W., Wei, X.-Y., Gong, Y., Ma, H.-Y., Zhang, Y.-L., Wen, X.-B., & Li, S.-K. (2018) · Developmental and Comparative Immunology · doi:10.1016/j.dci.2018.06.008 · Cited by 50 · see citing works
Transcriptome analysis identifies immune-related genes and antimicrobial peptides in Siamese fighting fish (Betta splendens)
Amparyup, P., Charoensapsri, W., Samaluka, N., Chumtong, P., Yocawibun, P., & Imjongjirak, C. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.02.030 · Cited by 48 · see citing works
Marine Arthropods as a Source of Antimicrobial Peptides
Saucedo-Vázquez, J. P., Gushque, F., Vispo, N. S., Rodríguez, J. A., Gomezjurado, M. E. G., Alberício, F., Tellkamp, M. P., & Alexis, F. (2022) · Marine Drugs · doi:10.3390/md20080501 · Cited by 48 · see citing works
Orally administered nano-polystyrene caused vitellogenin alteration and oxidative stress in the red swamp crayfish (Procambarus clarkii)
Capanni, F., Greco, S., Tomasi, N., Giulianini, P. G., & Manfrin, C. (2021) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2021.147984 · Cited by 46 · see citing works
The Anti-lipopolysaccharide Factors in Crustaceans
Li, S., & Li, F. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-41769-7_3 · Cited by 44 · see citing works
Armadillidin H, a Glycine-Rich Peptide from the Terrestrial Crustacean Armadillidium vulgare, Displays an Unexpected Wide Antimicrobial Spectrum with Membranolytic Activity
Verdon, J., Coutos‐Thévenot, P., Rodier, M., Landon, C., Depayras, S., Noël, C., Camera, S. L., Moumen, B., Grève, P., Bouchon, D., et al. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01484 · Cited by 43 · see citing works
Characterization of a type-I crustin with broad-spectrum antimicrobial activity from red swamp crayfish Procambarus clarkii
Liu, N., Zhang, R., Fan, Z.-X., Zhao, X., Wang, X., & Wang, J. (2016) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2016.03.025 · Cited by 41 · see citing works
Specific molecular signatures for type ii crustins in penaeid shrimp uncovered by the identification of crustin-like antimicrobial peptides in Litopenaeus vannamei
Barreto, C., Coelho, J., Yuan, J., Xiang, J., Perazzolo, L., & Rosa, R. (2018) · Marine Drugs · doi:10.3390/md16010031 · Cited by 40 · see citing works
“in non-decapod species, such as amphipods, copepods and isopods, and even in some hymenopteran insects [1].”
Background
A new antimicrobial peptide SCY2 identified in Scylla Paramamosain exerting a potential role of reproductive immunity
Qiao, K., Xu, W.-F., Chen, H., Peng, H., Zhang, Y., Huang, W., Wang, S., An, Z., Shan, Z., Chen, F., et al. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.02.022 · Cited by 39 · see citing works
PcToll3 was involved in anti- Vibrio response by regulating the expression of antimicrobial peptides in red swamp crayfish, Procambarus clarkii
Lan, J.-F., Wei, S., Wang, Y., Dai, Y., Tu, J., Zhao, L., Li, X.-C., Qin, Q., Chen, N., & Lin, L. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.08.021 · Cited by 38 · see citing works
Participation of lectins in crustacean immune system
Sánchez‐Salgado, J. L., Pereyra, A., Agundis, C., Vivanco-Rojas, Ó., Sierra-Castillo, C., Alpuche, J. J., & Zenteno, E. (2017) · Aquaculture Research · doi:10.1111/are.13394 · Cited by 37 · see citing works
Characterization and antimicrobial evaluation of Sp PR-AMP1, a proline-rich antimicrobial peptide from the mud crab Scylla paramamosain
Imjongjirak, C., Amphaiphan, P., Charoensapsri, W., & Amparyup, P. (2017) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2017.05.003 · Cited by 36 · see citing works
Newly identified type II crustin (SpCrus2) in Scylla paramamosain contains a distinct cysteine distribution pattern exhibiting broad antimicrobial activity
Wang, H., Zhang, J., Wang, Y., Fang, W., Wang, Y., Zhou, J.-F., Zhao, S., & Li, X.-C. (2018) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2018.01.021 · Cited by 36 · see citing works
Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus amphitrite
Zhang, W., Xu, X., Zhang, J., Ye, T., Zhou, Q., Xu, Y., Li, W., Hu, Z., & Shang, C. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14020413 · Cited by 35 · see citing works
CqToll participates in antiviral response against white spot syndrome virus via induction of anti-lipopolysaccharide factor in red claw crayfish Cherax quadricarinatus
Li, Y.-Y., Chen, X., Lin, F., Chen, Q.-F., Ma, X., & Liu, H.-P. (2017) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2017.04.020 · Cited by 34 · see citing works
Extracellular Vesicles and Post-Translational Protein Deimination Signatures in Mollusca—The Blue Mussel (Mytilus edulis), Soft Shell Clam (Mya arenaria), Eastern Oyster (Crassostrea virginica) and Atlantic Jacknife Clam (Ensis leei)
Bowden, T. J., Kraev, I., & Lange, S. (2020) · Biology · doi:10.3390/biology9120416 · Cited by 34 · see citing works
Antimicrobial Peptides and Ectosymbiotic Relationships: Involvement of a Novel Type IIa Crustin in the Life Cycle of a Deep-Sea Vent Shrimp
Le Bloa, S., Boidin-Wichlacz, C., Cueff-Gauchard, V., Rosa, R. D., Cuvillier-Hot, V., Durand, L., Methou, P., Pradillon, F., Cambon-Bonavita, M.-A., & Tasiemski, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01511 · Cited by 30 · see citing works
Unusual tissue distribution of carcinin, an antibacterial crustin, in the crab, Carcinus maenas, reveals its multi-functionality
Suleiman, S., Smith, V. J., & Dyrynda, E. A. (2017) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2017.06.010 · Cited by 32 · see citing works
Self-citation
Host-pathogen coevolution drives innate immune response to Aphanomyces astaci infection in freshwater crayfish: transcriptomic evidence
Boštjančić, L. L., Francesconi, C., Rutz, C., Hoffbeck, L., Poidevin, L., Kress, A., Jussila, J., Makkonen, J., Feldmeyer, B., Bálint, M., et al. (2022) · BMC Genomics · doi:10.1186/s12864-022-08571-z · Cited by 32 · see citing works
Next-Generation Sequencing and the Crustacean Immune System: The Need for Alternatives in Immune Gene Annotation.
Clark, K. F., & Greenwood, S. (2016) · Integrative and Comparative Biology · doi:10.1093/icb/icw023 · Cited by 30 · see citing works
Uncovering and defragmenting the role of the Toll pathway in the innate immune responses of cultured crustaceans against viral pathogens
Sánchez‐Paz, A., & Muhlia‐Almazán, A. (2020) · Reviews in Aquaculture · doi:10.1111/raq.12411 · Cited by 31 · see citing works
Shrimp Intestinal Microbiota Homeostasis: Dynamic Interplay Between the Microbiota and Host Immunity
Zhou, K., Liu, P., Yao, J., Vasta, G. R., Wang, J., & Wang, X. (2024) · Reviews in Aquaculture · doi:10.1111/raq.12986 · Cited by 30 · see citing works
Extracellular vesicles and post-translational protein deimination signatures in haemolymph of the American lobster (Homarus americanus).
Bowden, T., Kraev, I., & Lange, S. (2020) · Fish and Shellfish Immunology · doi:10.1016/j.fsi.2020.06.053 · Cited by 28 · see citing works
Identification and characterization of two arasin-like peptides in red swamp crayfish Procambarus clarkii
Chai, L., Li, W.-W., & Wang, X. (2017) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2017.09.059 · Cited by 28 · see citing works
Insights into Chagas treatment based on the potential of bacteriocin AS-48
Martín‐Escolano, R., Cebrián, R., Martín‐Escolano, J., Rosales, M. J., Maqueda, M., Sánchez‐Moreno, M., & Marı́n, C. (2019) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2019.03.003 · Cited by 28 · see citing works
Machine learning and genetic algorithm-guided directed evolution for the development of antimicrobial peptides
Zhang, H., Wang, Y., Zhu, Y., Huang, P., Gao, Q., Li, X., Chen, Z., Liu, Y., Jiang, J., Gao, Y., et al. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.02.016 · Cited by 29 · see citing works
Paralithocins, Antimicrobial Peptides with Unusual Disulfide Connectivity from the Red King Crab,Paralithodes camtschaticus
Moe, M. K., Haug, T., Sydnes, M. O., Sperstad, S. V., Li, C., Vaagsfjord, L. C., de la Vega, E., & Stensvåg, K. (2018) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00780 · Cited by 25 · see citing works
On the wave of the crustin antimicrobial peptide family: From sequence diversity to function
Barreto, C., Matos, G. M., & Rosa, R. D. (2022) · Fish and Shellfish Immunology Reports · doi:10.1016/j.fsirep.2022.100069 · Cited by 25 · see citing works
A Type IIa crustin from the pink shrimp Farfantepenaeus paulensis (crusFpau) is constitutively synthesized and stored by specific granule-containing hemocyte subpopulations
Bandeira, P. T., Vernal, J. I., Matos, G. M., Farias, N. D., Terenzi, H. F., Pinto, A. R., Barracco, M. A., & Rosa, R. D. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.12.055 · Cited by 25 · see citing works
Toxic effects of nanopolystyrene and cadmium on the intestinal tract of the Chinese mitten crab (Eriocheir sinensis)
Che, S., Huang, M., Ma, H., Wan, Z., Feng, J., Ding, S., & Li, X. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.115936 · Cited by 24 · see citing works
The potential of antimicrobial peptides isolated from freshwater crayfish species in new drug development: A review
Punginelli, D., Schillaci, D., Mauro, M., Deidun, A., Barone, G., Arizza, V., & Vazzana, M. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.104258 · Cited by 24 · see citing works
Harnessing marine antimicrobial peptides for novel therapeutics: A deep dive into ocean-derived bioactives
Kanaujia, K. A., Wagh, S. S., Pandey, G., Phatale, V., Khairnar, P., Kolipaka, T., Rajinikanth, P. S., Saraf, S. A., Srivastava, S. K., & Kumar, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142158 · Cited by 23 · see citing works
Crustin Defense against Vibrio parahaemolyticus Infection by Regulating Intestinal Microbial Balance in Litopenaeus vannamei
Lv, X., Li, S., Yu, Y., Zhang, X., & Li, F. (2023) · Marine Drugs · doi:10.3390/md21020130 · Cited by 23 · see citing works
Identification of a group D anti-lipopolysaccharide factor (ALF) from kuruma prawn (Marsupenaeus japonicus) with antibacterial activity against Vibrio parahaemolyticus
Zhang, H., Cheng, W., Zheng, L., Wang, P., Liu, Q., Li, Z., Li, T., Wei, Y., Mao, Y., & Yu, X. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.04.039 · Cited by 22 · see citing works
Comparative transcriptomics reveals the immune dynamics during the molting cycle of swimming crab Portunus trituberculatus
Liu, M., Ni, H., Zhang, X., Sun, Q., Wu, X., & He, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1037739 · Cited by 21 · see citing works
The chemo enzymatic functionalization of chitosan zeolite particles provides antioxidant and antimicrobial properties
Tegl, G., Stagl, V., Mensah, A., Huber, D., Somitsch, W., Grosse-Kracht, S., & Guebitz, G. M. (2018) · Engineering in Life Sciences · doi:10.1002/elsc.201700120 · Cited by 21 · see citing works
Cloning and Characterization of Two Toll Receptors (PcToll5 and PcToll6) in Response to White Spot Syndrome Virus in the Red Swamp Crayfish Procambarus clarkii
Huang, Y., Chen, Y.-H., Hui, K.-M., & Ren, Q. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00936 · Cited by 21 · see citing works
SpCrus3 and SpCrus4 share high similarity in mud crab (Scylla paramamosain) exhibiting different antibacterial activities
Wang, Y., Zhang, X., Wang, H., Fang, W., Ma, H., Zhang, F., Wang, Y., & Li, X.-C. (2018) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2018.01.006 · Cited by 20 · see citing works
Chromatin extracellular trap release in rainbow trout, Oncorhynchus mykiss (Walbaum, 1792)
Van, A. P., de Haro, N. Á., Bron, J. E., & Desbois, A. P. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.01.040 · Cited by 20 · see citing works
Effects of dietary glycerol monolaurate on growth and digestive performance, lipid metabolism, immune defense and gut microbiota of shrimp (Penaeus vannamei)
Liu, R., Ding, Y., Jing, F., Chen, Z., Su, C., & Pan, L. (2024) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2024.109666 · Cited by 18 · see citing works
Characterization of the Dual Functions of LvCrustinVII from Litopenaeus vannamei as Antimicrobial Peptide and Opsonin
Hu, J. H., Li, S., Lv, Q., Miao, M., Li, X., & Li, F. (2022) · Marine Drugs · doi:10.3390/md20030157 · Cited by 15 · see citing works
Redclaw crayfish (Cherax quadricarinatus) responds to Vibrio parahaemolyticus infection by activating toll and immune deficiency signaling pathways and transcription of associated immune response genes
Chen, D., & Wang, H. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.06.069 · Cited by 15 · see citing works
Extracellular Vesicle Signatures and Post-Translational Protein Deimination in Purple Sea Urchin (Strongylocentrotus purpuratus) Coelomic Fluid—Novel Insights into Echinodermata Biology
D’Alessio, S., Buckley, K. M., Kraev, I., Hayes, P. M., & Lange, S. (2021) · Biology · doi:10.3390/biology10090866 · Cited by 15 · see citing works
Post-translational protein deimination signatures in sea lamprey (Petromyzon marinus) plasma and plasma-extracellular vesicles
Rast, J. P., D’Alessio, S., Kraev, I., & Lange, S. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.104225 · Cited by 13 · see citing works
Recombinant expression of an oriental river prawn anti-lipopolysaccharide factor gene in Pichia pastoris and its characteristic analysis
Tang, T., Liu, J., Li, S., Li, H., & Liu, F. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.01.030 · Cited by 13 · see citing works
Shedding Light on the Antimicrobial Peptide Arsenal of Terrestrial Isopods: Focus on Armadillidins, a New Crustacean AMP Family
Becking, T., Delaunay, C., Cordaux, R., Berjeaud, J., Braquart‐Varnier, C., & Verdon, J. (2020) · Genes · doi:10.3390/genes11010093 · Cited by 13 · see citing works
Farfantepenaeus gene-encoded antimicrobial peptides: Identification, molecular characterization and gene expression in response to fungal infections
Machado, L. G., Gonçalves, P., Barreto, C., Perazzolo, L. M., & Rosa, R. D. (2021) · Journal of Invertebrate Pathology · doi:10.1016/j.jip.2021.107586 · Cited by 12 · see citing works
Transcriptional Identification of Related Proteins in the Immune System of the Crayfish Procambarus clarkii
Calderón‐Rosete, G., González-Barrios, J. A., Lara-Lozano, M., Piña-Leyva, C., & Rodríguez‐Sosa, L. (2018) · Microarrays · doi:10.3390/ht7030026 · Cited by 11 · see citing works
Antimicrobial peptides of invertebrates. Part 2. biological functions and mechanisms of action
Баландин, С. В., & Ovchinnikova, T. V. (2016) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s106816201604004x · Cited by 11 · see citing works
Characterization of the antibacterial and opsonic functions of the antimicrobial peptide LvCrustinVI from Litopenaeus vannamei
Hu, J. H., Li, S., Miao, M., & Li, F. (2024) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2024.105146 · Cited by 10 · see citing works
Identification and function of an Arasin-like peptide from Litopenaeus vannamei
Zhang, S., Hou, C., Xiao, B., Yao, Y., Xiao, W. L., Li, C., & Shi, L. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.104174 · Cited by 10 · see citing works
Manano oligosacaridos como prebioticos en acuicultura de crustaceos
Gainza, O., & Romero, J. (2017) · Latin American Journal of Aquatic Research · doi:10.3856/vol45-issue2-fulltext-2 · Cited by 9 · see citing works
A positive feedback loop between two C-type lectins originated from gene duplication and relish promotes the expression of antimicrobial peptides in Procambarus clarkii
Dai, X., Sun, M., Nie, X., Zhao, Y., Xu, H., Han, Z., Gao, T., Huang, X. H., & Ren, Q. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1021121 · Cited by 8 · see citing works
Characterization of the mature form of a β-defensin-like peptide, Hoa-D1, in the lobster Homarus americanus
Vu, G. H., Do, D., Rivera, C. D., Dickinson, P. S., Christie, A. E., & Stemmler, E. A. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.07.004 · Cited by 8 · see citing works
First identification and characterization of a triple WAP domain containing protein in Procambarus clarkii provides new insights into the classification and evolution of WAP proteins in crustacean
Zhang, Y., Wang, J., & Wang, X. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.09.023 · Cited by 7 · see citing works
A novel type II crustin in the innate immune response of the freshwater crab (Sinopotamon henanense) against infection and its expression changes by cadmium
Bao, M., Liang, Y., Lang, L., Chen, C. M., Zhang, Z., & Wang, L. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.108559 · Cited by 6 · see citing works
Functional analysis and modification of anti-lipopolysaccharide factor (ALF) from the freshwater crab Sinopotamon henanense and preparation of a novel ShALF6-2 K-AgNPs complex
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Proteomics of the haemolymph of the terrestrial crustacean Porcellio scaber reveals components of its innate immunity under baseline conditions
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Authors: Smith, V. J., & Dyrynda, E. A.
Affiliations: University of St Andrews (GB)
Heriot-Watt University (GB)
Corresponding author: Smith, Valerie J.
Venue: Molecular Immunology
Publisher: Elsevier BV
Published: 2015-12
Volume: 68
Issue: 2
Pages: 383-398
ISSN: 0161-5890 (ISSN-L)
DOI: 10.1016/j.molimm.2015.08.009
OpenAlex: W1193509026
Cited by: 85
References: 177
Citations by year: 2026: 3 · 2025: 4 · 2024: 8 · 2023: 4 · 2022: 10 · 2021: 10 · 2020: 13 · 2019: 6 · 2018: 10 · 2017: 6 · 2016: 11
FWCI: 1.10
Type: journal article
Language: en
Open access: green
hdl.handle.net
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Molecular Immunology (publishedVersion)
PubMed (publishedVersion)
St Andrews Research Repository (St Andrews Research Repository) (submittedVersion)
Funders: Biotechnology and Biological Sciences Research Council (BB/M026132/1)
Topics: Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
Life Sciences › Immunology and Microbiology › Immunology › Aquaculture disease management and microbiota
Keywords: antimicrobial peptides, crustacean innate immunity, Decapoda, shrimp, crayfish, crabs, lobster, gene expression, immune challenge, protease inhibition, phagocytosis, antiviral activity, hematopoiesis, host defense
MeSH terms: Animals, Anti-Infective Agents, Brachyura, Astacoidea, Microbial Sensitivity Tests, Muramidase, Shellfish, Antimicrobial Cationic Peptides, Penaeidae, Arthropod Proteins

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