Antibodies to the HIV-1 p17 Protein Cross-React with Human Superoxide Dismutase-2

Kato, Takeshi; Suzuki, Jun–ichi; Daimon, Makoto; Sasaki, Hideo; Ishikawa, Kiichi

doi:10.1006/bbrc.1996.5888

Cited by 4 publications

(2 citation statements)

References 21 publications

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“…brane segments were excluded. The level of similarity of the majority of regions shown in Tables 2-5 exceeds that of many regions whose cross-reactivity was demonstrated experimentally (Chen et al, 1997/98;Dyrberg and Oldstone, 1986;Evans and Levy, 1989;Kato et al, 1997;Solinema and De Camilli, 1995;Powell et al, 2000;Zagury et al, 1993a;Zagury et al, 1993b). For comparison, Table 6 shows some locally similar regions of HIV-1 and human proteins for which cross-reactivity was proved experimentally.…”

Section: Revealing Hiv-1 Protein Fragments Highly Similar To Human Prmentioning

confidence: 88%

Exclusion of HIV epitopes shared with human proteins is prerequisite for designing safer AIDS vaccines

Maksyutov

Bachinskii

Bazhan

et al. 2004

Journal of Clinical Virology

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Section: Revealing Hiv-1 Protein Fragments Highly Similar To Human Prmentioning

confidence: 88%

Exclusion of HIV epitopes shared with human proteins is prerequisite for designing safer AIDS vaccines

Maksyutov

Bachinskii

Bazhan

et al. 2004

Journal of Clinical Virology

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“…Taken together, these results suggest that the cross-reactivity of P30-52 MAb against Env V3 may depend on the structural similarity of the epitope regions of P30-52 and Env V3, and that Env V3 MAb also cross-reacts against P30-52. When we compared the three-dimensional structure of P30-52 with that of Env V3 reported by Massiah (30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40)(41)(42)(43) and H3 helix'47"52' and a part of H3 helix, and hence the highly conserved GPGRAF sequence of Env V3 adopts an S-shaped conformation. Thus, the FAVNPG'44^9' sequence of P30-52 and the GPGRAF sequence of Env V3 are quite similar in structure.…”

Section: Discussionmentioning

confidence: 99%

Anti-P30-52 Monoclonal Antibody Cross-Reacted to Env V3 and Inhibited the Viral Multiplication of HIV-1-Infected MT-4 Cells

Ota

Bautista²,

Yadav³

et al. 1999

Hybridoma

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It is well known that the anti-p17 antibody titer decreases with the disease progression among human immunodeficiency virus type 1 (HIV-1) carriers. We previously established several murine anti-p17 monoclonal antibodies (MAbs) to investigate the immunological role of p17, and to further characterize these MAbs, we examined the anti-p17 antibody titer in serum of a patient who was a long-term nonprogressor with hemophilia, and found that the antibody for the p17-derivative peptide from amino acid residues 30 to 52 (P30-52) cross-reacted to the third variable region of the envelope glycoprotein of HIV-1, Env V3. In the present study, we primed mice with P30-52 to establish anti-P30-52 MAbs (P30-52 MAbs), and examined their affinity and whether they suppressed the viral multiplication of HIV-1-infected MT-4 (HTLV-1-transformed CD4+ T-cell line) cells, in a TCID50 assay. At the same time, an anti-Env V3 MAb (Env V3 MAb) was also established and examined as above. The IgM-type P30-52 MAb and Env V3 MAb showed heteroclitic binding, and the IgM-type P30-52 MAb inhibited the viral multiplication. We also found that an increase of fragmented DNA of HIV-1-infected MT-4 cells co-cultured with P30-52 MAbs. Because DNA fragmentation is one of the features of programmed cell death, the viral multiplication may be suppressed by the apoptosis of HIV-1-infected MT-4 cells co-cultured with P30-52 MAbs. Though the relationship between cross-reactivity and the inhibition mechanism of multiplication of HIV-1 is unclear, P30-52 of p17 may well be a useful region of viral proteins for the development of therapeutic and vaccination strategies.

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Antibodies to the HIV-1 p17 Protein Cross-React with Human Superoxide Dismutase-2

Cited by 4 publications

References 21 publications

Exclusion of HIV epitopes shared with human proteins is prerequisite for designing safer AIDS vaccines

Exclusion of HIV epitopes shared with human proteins is prerequisite for designing safer AIDS vaccines

Anti-P30-52 Monoclonal Antibody Cross-Reacted to Env V3 and Inhibited the Viral Multiplication of HIV-1-Infected MT-4 Cells

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