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Electron microscopic evidence for the association of M 2 protein with the influenza virion

Identifieur interne : 002054 ( Main/Exploration ); précédent : 002053; suivant : 002055

Electron microscopic evidence for the association of M 2 protein with the influenza virion

Auteurs : D. C. Jackson [Australie] ; Xi-Lin Tang [Australie] ; K. Gopal Murti [États-Unis] ; R. G. Webster [États-Unis] ; G. W. Tregear [Australie] ; W. J. Bean [États-Unis]

Source :

RBID : ISTEX:4E540331DBE634F69C7AA7974D51574C11F4945A

English descriptors

Abstract

Summary: Immunogold electron microscopy revealed that site-specific antibodies elicited by a synthetic peptide representing the N-terminal sequence (residues 2–10) of influenza virus M 2 protein were capable of binding to the surface of virions. Antibody binding was observed with two human influenza virus strains but not with an avian virus strain which has amino acid substitutions in the appropriate sequence of M 2. These results provide direct evidence for the presence of M 2 in the influenza virion.

Url:
DOI: 10.1007/BF01314030


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<term>Proc natl acad</term>
<term>Rabbit antiserum</term>
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<div type="abstract" xml:lang="en">Summary: Immunogold electron microscopy revealed that site-specific antibodies elicited by a synthetic peptide representing the N-terminal sequence (residues 2–10) of influenza virus M 2 protein were capable of binding to the surface of virions. Antibody binding was observed with two human influenza virus strains but not with an avian virus strain which has amino acid substitutions in the appropriate sequence of M 2. These results provide direct evidence for the presence of M 2 in the influenza virion.</div>
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