Immunological cross-reactivity against a drug mutated HIV-1 protease epitope after DNA multi-CTL epitope construct immunization.

Abstract:

:Epitopes in HIV polymerase were analyzed by peptide binding to human leukocyte antigen (HLA) A0201 molecules, the most frequent HLA class in the Caucasian population. We found that HIV-1 protease peptides representing both the wild type and anticipated drug resistance variants of the sequence bound well to HLA-A0201. We also found that wild type as well as a double mutated variant of the epitope was strongly immunogenic in HLA-A0201 transgenic mice, either as individual peptides or encoded in DNA multi-CTL epitope constructs. Immunological cross-reactivity between different variants of the peptide could be seen, suggesting that it may be possible to induce a broad immune response by immunizing with drug resistance-mutated epitopes. This may be of advantage for HIV-1 infected patients since such a response may cause a better outcome of an anti-retroviral drug therapy.

journal_name

Vaccine

journal_title

Vaccine

authors

Boberg A,Sjöstrand D,Rollman E,Hinkula J,Zuber B,Wahren B

doi

10.1016/j.vaccine.2005.08.019

subject

Has Abstract

pub_date

2006-05-22 00:00:00

pages

4527-30

issue

21

eissn

0264-410X

issn

1873-2518

pii

S0264-410X(05)00815-7

journal_volume

24

pub_type

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