PMID- 11074471
OWN - NLM
STAT- MEDLINE
DCOM- 20010125
LR  - 20190831
IS  - 0146-6615 (Print)
IS  - 0146-6615 (Linking)
VI  - 62
IP  - 4
DP  - 2000 Dec
TI  - Increased immunoglobulin G, but not M, binding to endogenous retroviral antigens 
      in HIV-1 infected persons.
PG  - 435-44
AB  - The modes of interaction between products of human endogenous retroviral (HERV) 
      sequences and the immune system are largely unknown. In HIV infected persons, an 
      exogenous retrovirus adds further complexity to the situation. Therefore, 14 
      synthetic peptides with sequences derived from conserved regions of various 
      endogenous retroviruses (ERVs) and from related exogenous retroviruses were used 
      to search for IgG and IgM antibodies that bind to such antigens in 15 HIV-1 
      seropositive and 17 seronegative immunosuppressed patients. IgG binding to three 
      peptides, namely, the C-terminal half of murine leukemia virus (MLV) capsid 
      protein, the conserved portion of HERV-H transmembrane protein, and the Pol 
      region of human mouse mammary tumor virus (MMTV)-like (HML3) sequence, was 
      observed in both groups. Binding was, however, more frequent and more firm in 
      HIV-1 positive samples (P<0.0001, Wilcoxon rank sum test). IgM binding to the 
      same peptides showed no significant differentiation between the two groups of 
      patients. Binding to both immunoglobulin isotypes was sometimes variable over 
      time in both groups. No correlation of either IgG or IgM peptide binding with 
      progression to AIDS in HIV-1 infected individuals was observed. Inhibition 
      studies using analogous endogenous and exogenous retroviral peptides, including 
      HIV-1, demonstrated specificity of the IgG antibodies for a narrow range of MLV- 
      and MMTV-like retroviral antigens, and excluded cross-reactivity of antibodies to 
      HIV-1 as a cause of these observations. Thus, unlike IgG, IgM binding to 
      retroviral antigens was ubiquitous. It is suggested that anti-HERV IgM belong to 
      a class of natural antibodies and might serve as primers in the mediation of 
      humoral immune responses to more or less related exogenous retroviruses. 
      Increased IgG binding in HIV-1 infected individuals could result from such 
      priming, or reflect higher HERV antigen expression.
CI  - Copyright 2000 Wiley-Liss, Inc.
FAU - Lawoko, A
AU  - Lawoko A
AD  - Department of Medical Sciences, Section of Virology, Uppsala Academic Hospital, 
      Uppsala, Sweden. alex.lawoko@telia.com
FAU - Johansson, B
AU  - Johansson B
FAU - Rabinayaran, D
AU  - Rabinayaran D
FAU - Pipkorn, R
AU  - Pipkorn R
FAU - Blomberg, J
AU  - Blomberg J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Med Virol
JT  - Journal of medical virology
JID - 7705876
RN  - 0 (Antibodies, Viral)
RN  - 0 (Antigens, Viral)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Retroviridae Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies, Viral/*immunology
MH  - Antigen-Antibody Reactions
MH  - Antigens, Viral/*immunology
MH  - Cross-Sectional Studies
MH  - Endogenous Retroviruses/*immunology
MH  - HIV Infections/blood/*immunology
MH  - HIV-1/*immunology
MH  - Humans
MH  - Immunocompromised Host/immunology
MH  - Immunoglobulin G/*immunology
MH  - Immunoglobulin M/*immunology
MH  - Longitudinal Studies
MH  - Mice
MH  - Molecular Sequence Data
MH  - Retroviridae/*immunology
MH  - Retroviridae Proteins/*immunology
EDAT- 2000/11/14 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/11/14 11:00
PHST- 2000/11/14 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/11/14 11:00 [entrez]
AID - 10.1002/1096-9071(200012)62:4<435::AID-JMV7>3.0.CO;2-R [pii]
AID - 10.1002/1096-9071(200012)62:4<435::aid-jmv7>3.0.co;2-r [doi]
PST - ppublish
SO  - J Med Virol. 2000 Dec;62(4):435-44. doi: 
      10.1002/1096-9071(200012)62:4<435::aid-jmv7>3.0.co;2-r.