DIFFERENTIAL-EFFECTS OF FLANKING RESIDUES ON PRESENTATION OF EPITOPES FROM CHIMERIC PEPTIDES

被引：38

作者：

BERGMANN, CC ^{[1
]}

TONG, LL ^{[1
]}

CUA, R ^{[1
]}

SENSINTAFFAR, J ^{[1
]}

STOHLMAN, S ^{[1
]}

机构：

[1] UNIV SO CALIF,SCH MED,DEPT MICROBIOL,LOS ANGELES,CA 90033

来源：

JOURNAL OF VIROLOGY | 1994年 / 68卷 / 08期

关键词：

D O I：

10.1128/JVI.68.8.5306-5310.1994

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Chimeric peptides in which the optimal H-2(d) mouse hepatitis virus nucleocapsid (pN) and human immunodeficiency virus type 1 (p18) epitopes, separated by 38, 7, or 2 amino acids, were expressed from a single open reading frame by using recombinant vaccinia viruses to analyze antigen processing of proximal class I-restricted epitopes. Recognition of the carboxy-terminal D-d-restricted p18 epitope was independent of the amino-terminal flanking residues. By contrast, proximity of the carboxy-terminal epitope decreased recognition of the amino-terminal L(d)-restricted pN epitope. Immunization resulted in the induction of both p18- and pN-specific antiviral cytotoxic T lymphocytes, irrespective of the number of amino acids separating the epitopes.

引用

页码：5306 / 5310

页数：5

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