Linked Life Data

19118511

Source:http://linkedlifedata.com/resource/pubmed/id/19118511

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-1-2
pubmed:abstractText
Hepatitis E virus (HEV) genotype 4 was originally identified in China. Its neutralization antigenic epitopes have not been characterized. Recently, we identified a neutralizing monoclonal antibody (mAb) 1G10, which was generated following immunization of mice with p166Chn, a recombinant protein comprising 464-629 amino acids (aa) of the HEV genotype 4 capsid protein. In this study, a panel of 22 N- and/or C-terminal truncated and 6 site-directed mutated p166Chn proteins were prepared. Only those N- or C-terminal truncated proteins containing the region 477-613 aa could react with the mAb 1G10, suggesting the neutralization epitope of HEV genotype 4 is located between aa477 and aa613. However, a both N- and C-terminal truncated protein, pN477-C613, neither reacted to 1G10 nor elicited neutralizing antibodies in mice, while another both terminal truncated protein, pN472-C617, did, suggesting the flanking regions of the pN477-C613 could help to stabilize and allow presentation of the neutralization epitope to the immune system. Substituting Leu477 and/or Leu613 with the polar, uncharged threonine (Thr) caused > or =50% reduction of the mutants' immunoreactivity to 1G10, whereas replacement by hydrophobic phenylalanine (Phe) made little impact on the immunoreactivity, revealing functional associations between hydrophobicity of aa at positions 477 and 613 and the antigenicity of p166Chn. These data suggested Leu477 and Leu613 are critical in forming the neutralization epitope of HEV genotype 4.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
2042-0226
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
447-56
pubmed:dateRevised
2010-3-15
pubmed:meshHeading
pubmed-meshheading:19118511-Animals, pubmed-meshheading:19118511-Antibodies, Monoclonal, pubmed-meshheading:19118511-Antibody Specificity, pubmed-meshheading:19118511-Antigens, Viral, pubmed-meshheading:19118511-Conserved Sequence, pubmed-meshheading:19118511-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:19118511-Epitope Mapping, pubmed-meshheading:19118511-Epitopes, pubmed-meshheading:19118511-Genotype, pubmed-meshheading:19118511-Hepatitis E virus, pubmed-meshheading:19118511-Immune Sera, pubmed-meshheading:19118511-Leucine, pubmed-meshheading:19118511-Mice, pubmed-meshheading:19118511-Mice, Inbred BALB C, pubmed-meshheading:19118511-Mutation, pubmed-meshheading:19118511-Neutralization Tests, pubmed-meshheading:19118511-Peptide Fragments, pubmed-meshheading:19118511-RNA, Viral, pubmed-meshheading:19118511-Recombinant Proteins, pubmed-meshheading:19118511-Viral Proteins
pubmed:year
2008
pubmed:articleTitle
The Leu477 and Leu613 of ORF2-encoded protein are critical in forming neutralization antigenic epitope of hepatitis E virus genotype 4.
pubmed:affiliation
Department of Microbiology and Immunology, Southeast University School of Medicine, Nanjing, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't