Influenza Virus Resistance to Human Neutralizing Antibodies

ABSTRACT The human antibody repertoire has an exceptionally large capacity to recognize new or changing antigens through combinatorial and junctional diversity established at the time of V(D)J recombination and through somatic hypermutation. Influenza viruses exhibit a relentless capacity to escape...

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Autor principal:	James E. Crowe
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2012
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/97c0e69f8fc845c2b02376dd37b584a0
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spelling	oai:doaj.org-article:97c0e69f8fc845c2b02376dd37b584a02021-11-15T15:39:10ZInfluenza Virus Resistance to Human Neutralizing Antibodies10.1128/mBio.00213-122150-7511https://doaj.org/article/97c0e69f8fc845c2b02376dd37b584a02012-08-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00213-12https://doaj.org/toc/2150-7511ABSTRACT The human antibody repertoire has an exceptionally large capacity to recognize new or changing antigens through combinatorial and junctional diversity established at the time of V(D)J recombination and through somatic hypermutation. Influenza viruses exhibit a relentless capacity to escape the human antibody response by altering the amino acids of their surface proteins in hypervariable domains that exhibit a high level of structural plasticity. Both parties in this high-stakes game of shape shifting drive structural evolution of their functional proteins (the B cell receptor/antibody on one side and the viral hemagglutinin and neuraminidase proteins on the other) using error-prone polymerase systems. It is likely that most of the genetic mutations that occur in these systems are deleterious, resulting in the failure of the B cell or virus with mutations to propagate in the immune repertoire or viral quasispecies. A subset of mutations is tolerated in functional surface proteins that enter the B cell or virus progeny pool. In both cases, selection occurs in the population of mutated and unmutated species. In cases where the functional avidity of the B cell receptor is increased significantly, that clone may be selected for preferential expansion. In contrast, an influenza virus that “escapes” the inhibitory effect of secreted antibodies may represent a high proportion of the progeny virus in that host. The recent paper by O’Donnell et al. [C. D. O’Donnell et al., mBio 3(3):e00120-12, 2012] identifies a mechanism for antibody resistance that does not require escape from binding but rather achieves a greater efficiency in replication.James E. CroweAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 3, Iss 4 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 James E. Crowe Influenza Virus Resistance to Human Neutralizing Antibodies
description	ABSTRACT The human antibody repertoire has an exceptionally large capacity to recognize new or changing antigens through combinatorial and junctional diversity established at the time of V(D)J recombination and through somatic hypermutation. Influenza viruses exhibit a relentless capacity to escape the human antibody response by altering the amino acids of their surface proteins in hypervariable domains that exhibit a high level of structural plasticity. Both parties in this high-stakes game of shape shifting drive structural evolution of their functional proteins (the B cell receptor/antibody on one side and the viral hemagglutinin and neuraminidase proteins on the other) using error-prone polymerase systems. It is likely that most of the genetic mutations that occur in these systems are deleterious, resulting in the failure of the B cell or virus with mutations to propagate in the immune repertoire or viral quasispecies. A subset of mutations is tolerated in functional surface proteins that enter the B cell or virus progeny pool. In both cases, selection occurs in the population of mutated and unmutated species. In cases where the functional avidity of the B cell receptor is increased significantly, that clone may be selected for preferential expansion. In contrast, an influenza virus that “escapes” the inhibitory effect of secreted antibodies may represent a high proportion of the progeny virus in that host. The recent paper by O’Donnell et al. [C. D. O’Donnell et al., mBio 3(3):e00120-12, 2012] identifies a mechanism for antibody resistance that does not require escape from binding but rather achieves a greater efficiency in replication.
format	article
author	James E. Crowe
author_facet	James E. Crowe
author_sort	James E. Crowe
title	Influenza Virus Resistance to Human Neutralizing Antibodies
title_short	Influenza Virus Resistance to Human Neutralizing Antibodies
title_full	Influenza Virus Resistance to Human Neutralizing Antibodies
title_fullStr	Influenza Virus Resistance to Human Neutralizing Antibodies
title_full_unstemmed	Influenza Virus Resistance to Human Neutralizing Antibodies
title_sort	influenza virus resistance to human neutralizing antibodies
publisher	American Society for Microbiology
publishDate	2012
url	https://doaj.org/article/97c0e69f8fc845c2b02376dd37b584a0
work_keys_str_mv	AT jamesecrowe influenzavirusresistancetohumanneutralizingantibodies
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Influenza Virus Resistance to Human Neutralizing Antibodies

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