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Structural basis of influenza virus neutralization

Identifieur interne : 000780 ( Pmc/Checkpoint ); précédent : 000779; suivant : 000781

Structural basis of influenza virus neutralization

Auteurs : Thomas Han ; Wayne A. Marasco

Source :

RBID : PMC:3062959

Abstract

Although seasonal influenza vaccines play a valuable role in reducing the spread of the virus at the population level, ongoing viral evolution to evade immune responses remains problematic. No current vaccines are likely to elicit enduring protection in the face of emerging and re-emerging influenza viruses that rapidly undergoing antigenic drift. Eliciting broadly cross-neutralizing antibody responses against influenza virus is a crucial goal for seasonal and pandemic influenza vaccine preparation. Recent three-dimensional structure information obtained from crystallization of influenza antigens in complex with neutralizing antibodies (nAbs) have provided a framework for interpreting antibody-based viral neutralization that should aid in the design of vaccine immunogens. Here, we will review current knowledge of the structure-based mechanisms contributing to the neutralization and neutralization escape of influenza viruses. We will also explore the potential for this structure-based approach to overcome the challenge of obtaining the highly desired “universal” influenza vaccine.


Url:
DOI: 10.1111/j.1749-6632.2010.05829.x
PubMed: 21251008
PubMed Central: 3062959


Affiliations:


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PMC:3062959

Le document en format XML

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<p id="P1">Although seasonal influenza vaccines play a valuable role in reducing the spread of the virus at the population level, ongoing viral evolution to evade immune responses remains problematic. No current vaccines are likely to elicit enduring protection in the face of emerging and re-emerging influenza viruses that rapidly undergoing antigenic drift. Eliciting broadly cross-neutralizing antibody responses against influenza virus is a crucial goal for seasonal and pandemic influenza vaccine preparation. Recent three-dimensional structure information obtained from crystallization of influenza antigens in complex with neutralizing antibodies (nAbs) have provided a framework for interpreting antibody-based viral neutralization that should aid in the design of vaccine immunogens. Here, we will review current knowledge of the structure-based mechanisms contributing to the neutralization and neutralization escape of influenza viruses. We will also explore the potential for this structure-based approach to overcome the challenge of obtaining the highly desired “universal” influenza vaccine.</p>
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<aff id="A1">Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Medicine, Harvard Medical School, Boston, Massachusetts, USA</aff>
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<corresp id="CR1">Corresponding author: Wayne A. Marasco, MD, PhD. Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, Boston, 44 Binney Street, Boston, Massachusetts 02115, USA,
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<p id="P1">Although seasonal influenza vaccines play a valuable role in reducing the spread of the virus at the population level, ongoing viral evolution to evade immune responses remains problematic. No current vaccines are likely to elicit enduring protection in the face of emerging and re-emerging influenza viruses that rapidly undergoing antigenic drift. Eliciting broadly cross-neutralizing antibody responses against influenza virus is a crucial goal for seasonal and pandemic influenza vaccine preparation. Recent three-dimensional structure information obtained from crystallization of influenza antigens in complex with neutralizing antibodies (nAbs) have provided a framework for interpreting antibody-based viral neutralization that should aid in the design of vaccine immunogens. Here, we will review current knowledge of the structure-based mechanisms contributing to the neutralization and neutralization escape of influenza viruses. We will also explore the potential for this structure-based approach to overcome the challenge of obtaining the highly desired “universal” influenza vaccine.</p>
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<contract-num rid="AI1">U01 AI074518-03 ||AI</contract-num>
<contract-sponsor id="AI1">National Institute of Allergy and Infectious Diseases Extramural Activities : NIAID</contract-sponsor>
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