Identification of critical contact residues in the NC41 epitope of a subtype N9 influenza virus neuraminidase
Identifieur interne : 001F09 ( Main/Exploration ); précédent : 001F08; suivant : 001F10Identification of critical contact residues in the NC41 epitope of a subtype N9 influenza virus neuraminidase
Auteurs : Jacqueline M. Nuss [États-Unis] ; Patricia Bossart Whitaker [États-Unis] ; Gillian M. Air [États-Unis]Source :
- Proteins: Structure, Function, and Bioinformatics [ 0887-3585 ] ; 1993-02.
English descriptors
- Teeft :
- Acid change, Amino, Amino acid, Amino acid substitutions, Amino acids, Antibody, Antibody binding, Antibody contacts, Antibody recognition, Assay, Biol, Complex formation, Contact residues, Critical contact residues, Critical contacts, Crystal structure, Crystal structures, Enzyme, Enzyme activity, Epitope, Heavy chain, Hydrogen bond, Immunoprecipitated, Influenza, Influenza virus, Influenza virus neuraminidase, Inhibition assays, Laver, Light chain, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Mutagenesis, Mutant, Neuraminidase, Polypeptide loops, Recombinant vaccinia virus, Residue, Salt link, Side chain, Side chains, Single change, Substitution, Varghese, Virology.
Abstract
We have examined amino acids on influenza virus neuraminidase (NA) subtype N9 (A/tern/Australia/G70c/75) which are in contact with monoclonal antibody NC41 to analyze individual interactions important for antibody recognition. The crystal structure of NA complexed with NC41 Fab1 shows antibody contacts at 19 amino acid residues on the NA surface which are localized on five polypeptide loops surrounding the enzyme active site. Fifteen mutant NA genes were constructed to encode a protein which contained a single amino acid substitution and these were tested for effects of the replacement on NC41 binding. Our data revealed that NAs with changes at 368, 400, and 434 completely lost NC41 recognition. NAs with side chains replaced at residues 346 and 373 exhibited binding reduced to less than 50% of wild‐type binding. Changes in seven other contacting residues, including substituted side chains which differed considerably from wild‐type NA in size and charge, had no significant effect on NC41 binding. These results indicate that only a few of the many residues which make up an epitope are crucial for interaction and provide the critical contacts required for antibody recognition. This implies that antibody escape mutants are selected only if they contain changes at these crucial sites, or changes which introduce bulky side chains that sterically prevent antibody attachment. © 1993 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/prot.340150204
Affiliations:
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Nuss</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Department of Microbiology, University of Alabama at Birmingham, Birmingham</wicri:cityArea></affiliation></author><author><name sortKey="Whitaker, Patricia Bossart" sort="Whitaker, Patricia Bossart" uniqKey="Whitaker P" first="Patricia Bossart" last="Whitaker">Patricia Bossart Whitaker</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Department of Microbiology, University of Alabama at Birmingham, Birmingham</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">New Jersey</region></placeName><wicri:cityArea>Current Address: Bristol‐Myers Squibb Pharmaceutical Research Institute, P.O. Box 4000, Department of Macromolecular Crystallography</wicri:cityArea></affiliation></author><author><name sortKey="Air, Gillian M" sort="Air, Gillian M" uniqKey="Air G" first="Gillian M." last="Air">Gillian M. Air</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Department of Microbiology, University of Alabama at Birmingham, Birmingham</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Correspondence address: Department of Microbiology, The University of Alabama at Birmingham, Basic Health Science Bldg., Room 360, UAB Station, Birmingham</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Proteins: Structure, Function, and Bioinformatics</title><title level="j" type="alt">PROTEINS: STRUCTURE, FUNCTION, AND BIOINFORMATICS</title><idno type="ISSN">0887-3585</idno><idno type="eISSN">1097-0134</idno><imprint><biblScope unit="vol">15</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="121">121</biblScope><biblScope unit="page" to="132">132</biblScope><biblScope unit="page-count">12</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1993-02">1993-02</date></imprint><idno type="ISSN">0887-3585</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0887-3585</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acid change</term><term>Amino</term><term>Amino acid</term><term>Amino acid substitutions</term><term>Amino acids</term><term>Antibody</term><term>Antibody binding</term><term>Antibody contacts</term><term>Antibody recognition</term><term>Assay</term><term>Biol</term><term>Complex formation</term><term>Contact residues</term><term>Critical contact residues</term><term>Critical contacts</term><term>Crystal structure</term><term>Crystal structures</term><term>Enzyme</term><term>Enzyme activity</term><term>Epitope</term><term>Heavy chain</term><term>Hydrogen bond</term><term>Immunoprecipitated</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Inhibition assays</term><term>Laver</term><term>Light chain</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Mutagenesis</term><term>Mutant</term><term>Neuraminidase</term><term>Polypeptide loops</term><term>Recombinant vaccinia virus</term><term>Residue</term><term>Salt link</term><term>Side chain</term><term>Side chains</term><term>Single change</term><term>Substitution</term><term>Varghese</term><term>Virology</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have examined amino acids on influenza virus neuraminidase (NA) subtype N9 (A/tern/Australia/G70c/75) which are in contact with monoclonal antibody NC41 to analyze individual interactions important for antibody recognition. The crystal structure of NA complexed with NC41 Fab1 shows antibody contacts at 19 amino acid residues on the NA surface which are localized on five polypeptide loops surrounding the enzyme active site. Fifteen mutant NA genes were constructed to encode a protein which contained a single amino acid substitution and these were tested for effects of the replacement on NC41 binding. Our data revealed that NAs with changes at 368, 400, and 434 completely lost NC41 recognition. NAs with side chains replaced at residues 346 and 373 exhibited binding reduced to less than 50% of wild‐type binding. Changes in seven other contacting residues, including substituted side chains which differed considerably from wild‐type NA in size and charge, had no significant effect on NC41 binding. These results indicate that only a few of the many residues which make up an epitope are crucial for interaction and provide the critical contacts required for antibody recognition. This implies that antibody escape mutants are selected only if they contain changes at these crucial sites, or changes which introduce bulky side chains that sterically prevent antibody attachment. © 1993 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Alabama</li><li>New Jersey</li></region></list><tree><country name="États-Unis"><region name="Alabama"><name sortKey="Nuss, Jacqueline M" sort="Nuss, Jacqueline M" uniqKey="Nuss J" first="Jacqueline M." last="Nuss">Jacqueline M. Nuss</name></region><name sortKey="Air, Gillian M" sort="Air, Gillian M" uniqKey="Air G" first="Gillian M." last="Air">Gillian M. Air</name><name sortKey="Air, Gillian M" sort="Air, Gillian M" uniqKey="Air G" first="Gillian M." last="Air">Gillian M. Air</name><name sortKey="Whitaker, Patricia Bossart" sort="Whitaker, Patricia Bossart" uniqKey="Whitaker P" first="Patricia Bossart" last="Whitaker">Patricia Bossart Whitaker</name><name sortKey="Whitaker, Patricia Bossart" sort="Whitaker, Patricia Bossart" uniqKey="Whitaker P" first="Patricia Bossart" last="Whitaker">Patricia Bossart Whitaker</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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