Early development of anti-HIV IgG

Wahrén, Britta; Broliden, P A; Trojnar, Jerzy; Sölver, Ellen; Albert, Jan; Sandström, Eric; Sydowe, Madeleine von; Wigzell, Hans

doi:10.1007/978-94-010-9060-5_282

Cited by 3 publications

(5 citation statements)

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“…The C4 domain is immunogenic in HIV-infected humans, demonstrated by the reactivity of HIV-1+ sera with modified C4 peptides (43). Is it a domain relevant to virus neutralization in the natural humoral immune response to HIV-1 infection?…”

Section: Discussionmentioning

confidence: 99%

Immunochemical analysis of the gp120 surface glycoprotein of human immunodeficiency virus type 1: probing the structure of the C4 and V4 domains and the interaction of the C4 domain with the V3 loop

Moore

Thali

Jameson

et al. 1993

J Virol

131

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We have probed the structure of the C4 and V3 domains of human immunodeficiency virus type 1 gpl20 by immunochemical techniques. Monoclonal antibodies (MAbs) recognizing an exposed gpl20 sequence, (E/ K)VGKAAMYAPP, in C4 were differentially sensitive to denaturation of gpl20, implying a conformational component to some of the epitopes. The MAbs recognizing conformation-sensitive C4 structures failed to bind to a gpl20 mutant with an alteration in the sequence of the V3 loop, and their binding to gpl20 was inhibited by both V3 and C4 MAbs. This implies an interaction between the V3 and C4 regions of gpl20, which is supported by the observation that the binding of some MAbs to the V3 loop was often enhanced by amino acid changes in and around the C4 region.

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Section: Discussionmentioning

confidence: 99%

Immunochemical analysis of the gp120 surface glycoprotein of human immunodeficiency virus type 1: probing the structure of the C4 and V4 domains and the interaction of the C4 domain with the V3 loop

Moore

Thali

Jameson

et al. 1993

J Virol

131

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“…By using an analytical technique employing modified peptides, a strong and frequent reactivity of sera from infected persons was however revealed [54]. Our MoAb MO86 reacts strongly in this region.…”

Section: Discussionmentioning

confidence: 70%

Human MoAbs produced from normal, HIV-1-negative donors and specific for glycoprotein gp 120 of the HIV-1 envelope

Ohlin

Hinkula²,

Broliden³

et al. 1992

Clinical and Experimental Immunology

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SUMMARYHuman MoAbsof IgM class were developed against three regions of the HIV-1 envelope. Uninfeeted donor lymphocytes were immunized in vitro with recombinant protein pBI. Four out of five antibodies were directed to different parts ofthe V3 region, which contains a major neutralizing site. Two out of these antibodies were directed to more than one amino acid sequence, indicating reactivity to discontinuous sites. Two of the human MoAbs inhibited viral spread between cells in tissue culture, interpreted as reactivities to conserved amino acid sequences exposed during viral maturation. No MoAb neutralized virus, which may be explained by the relatively low avidity of the antibodies. One MoAb was directed to a region containing amino acids participating in CD4 binding. This technique appears to allow formation of antibodies with fine specificities other than those obtained in infected hosts.

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“…Using a different approach, a fourth immunodominant site was identified in the extreme carboxy-terminal end of gp 120 (amino acids 504-518) [17]. A highly reactive peptide also was generated by use of a sequence representing the middle part of the CD4-binding region (amino acids 427-448) [18]. In order to effectively detect these antibodies, it was necessary to change the Met in position 434 to a Cys and to make the peptide cyclic.…”

Section: Selection Of Epitopes Relevant For Hiv Diagnosismentioning

confidence: 99%

“…1 See footnote of from results of other studies [51] that a 'loop' formation by interaction between the two cysteines is important, and peptides with a stabilized 'loop' can be effectively employed [39,40], Anti-SIVmac peptide monoclonal antibod ies reacting with the site Trp596 to Glu602 ef fectively block the capacity of the peptide to react with human postinfection HIV type 2 antibodies, but no similar blocking is seen with monoclonal antibodies against other antigenic sites in the peptide [11], A cross reacting site involving amino acids Ala582 to Lys588/G lu 588 was identified with both hyper immune sera and monoclonal antibodies against the peptides. This site was not acces sible in the intact transmembrane proteins, as determined by ELISA and Western blot tests.…”

Section: -Q---s------vt-i-k--q--ar-ns---afrqv-h-t---vn0 -T---------e mentioning

confidence: 99%

“…Two approaches were taken to further im prove the sensitivity of the site-specific pep tide ELISA tests. These approaches were (1) to couple peptides to some compound facili tating their adsorption to the plastic surface [33,35,36] and (2) to cycle peptides for im provement of their antigenicity [33,39,40]. In one study [33], both methods were used.…”

Section: Practical Use Of Peptides For Hiv Diagnosismentioning

confidence: 99%

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Human Immunodeficiency Virus Antibody Responses Determined by Site-Directed Serology

Norrby¹

1990

Intervirology

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In this brief review, the use of synthetic peptides representing linear antigenic sites in human immunodeficiency virus (HIV) structural proteins for detection of antibodies in sera from HIV-infected individuals is discussed. It has been demonstrated that peptide antigens offer unique advantages for determination of HIV-specific antibodies. In particular, various peptides representing the region of amino acids 580–620 in the transmembranous glycoprotein have been effectively used. Of primary importance is the fact that properly designed site-specific serological tests allow a distinction between type-specific antibodies, a quality not provided by any other currently available test. Furthermore, synthetic peptide antigens allow the design of highly simplified and effectively standardized assays. Hereby, they lend themselves to use for screening purposes or confirmatory testings not only in industrialized countries, but also in developing countries. It is also possible that tests with selected peptides may measure antibodies which have value in predicting the risk for infection in children born to seropositive mothers and for progression of disease in infected individuals.

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Early development of anti-HIV IgG

Cited by 3 publications

References 4 publications

Immunochemical analysis of the gp120 surface glycoprotein of human immunodeficiency virus type 1: probing the structure of the C4 and V4 domains and the interaction of the C4 domain with the V3 loop

Immunochemical analysis of the gp120 surface glycoprotein of human immunodeficiency virus type 1: probing the structure of the C4 and V4 domains and the interaction of the C4 domain with the V3 loop

Human MoAbs produced from normal, HIV-1-negative donors and specific for glycoprotein gp 120 of the HIV-1 envelope

Human Immunodeficiency Virus Antibody Responses Determined by Site-Directed Serology

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