Linked Life Data

1688628

Source:http://linkedlifedata.com/resource/pubmed/id/1688628

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-2-14
pubmed:abstractText
Earlier studies of a group of monoclonal antibody-resistant (mar) mutants of herpes simplex virus type 1 glycoprotein C (gC) operationally defined two distinct antigenic sites on this molecule, each consisting of numerous overlapping epitopes. In this report, we further define epitopes of gC by sequence analysis of the mar mutant gC genes. In 18 mar mutants studied, the mar phenotype was associated with a single nucleotide substitution and a single predicted amino acid change. The mutations were localized to two regions within the coding sequence of the external domain of gC and correlated with the two previously defined antigenic sites. The predicted amino acid substitutions of site I mutants resided between residues Gln-307 and Pro-373, whereas those of site II mutants occurred between amino acids Arg-129 and Glu-247. Of the 12 site II mutations, 9 induced amino acid substitutions within an arginine-rich segment of 8 amino acids extending from residues 143 to 151. The clustering of the majority of substituted residues suggests that they contribute to the structure of the affected sites. Moreover, the patterns of substitutions which affected recognition by antibodies with similar epitope specificities provided evidence that epitope structures are physically linked and overlap within antigenic sites. Of the nine epitopes defined on the basis of mutations, three were located within site I and six were located within site II. Substituted residues affecting the site I epitopes did not overlap substituted residues of site II, supporting our earlier conclusion that sites I and II reside in spatially distinct antigenic domains. A computer analysis of the distribution of charged residues and the predicted secondary structural features of wild-type gC revealed that the two antigenic sites reside within the most hydrophilic regions of the molecule and that the antigenic residues are likely to be organized as beta sheets which loop out from the surface of the molecule. Together, these data and our previous studies support the conclusion that the mar mutations identified by sequence analysis very likely occur within or near the epitope structures themselves. Thus, two highly antigenic regions of gC have now been physically and genetically mapped to well-defined domains of the protein molecule.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-2415719, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-2423702, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-2463380, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-2578193, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-2582051, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-2824652, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-2845681, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-3006335, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-3009845, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-3018078, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-3025606, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-3035578, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-3037106, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-3518749, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-388356, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-4125509, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-4705382, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6092678, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6092712, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6097034, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6187935, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6209578, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6252331, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6264114, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6269464, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6277790, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6300426, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6302327, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6311910, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6328323, http://linkedlifedata.com/resource/pubmed/commentcorrection/1688628-6969228
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
856-63
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Characterization of the antigenic structure of herpes simplex virus type 1 glycoprotein C through DNA sequence analysis of monoclonal antibody-resistant mutants.
pubmed:affiliation
Department of Human Genetics, University of Michigan Medical School, Ann Arbor 48109.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.