Reciprocal cytotoxic T lymphocyte cross-reactivity interactions between two major epitopes within HIV-1 gp160.

Important note: Information in this article was accurate in 1997. The state of the art may have changed since the publication date.

Reciprocal cytotoxic T lymphocyte cross-reactivity interactions between two major epitopes within HIV-1 gp160.

J Immunol. 1996 Nov 15;157(10):4399-411. Unique Identifier : AIDSLINE MED/97064196
Shirai M; Kurokohchi K; Pendleton CD; Arichi T; Boyd LF; Takahashi H; Margulies DH; Berzofsky JA; Molecular Immunogenetics and Vaccine Research Section, National; Cancer Institute, Bethesda, MD 20892, USA.

Abstract: We have observed and analyzed an unexpected cross-reactivity of CD8+ CTL between two nonhomologous peptides of the HIV-1 IIIB gp160 envelope protein, P18 (residues 315-329) and HP53 (834-848, also called TH4.1), in the context of four different class I MHC molecules, Dd, Dp, Dq (or Lq), and H-2u. In strains expressing Dd, the cross-reactivity between peptides was bidirectional, whereas in other strains (H-2u, H-2p, and H-2q), the cross-reactivity was unidirectional; that is, P18-specific CTLs showed no killing against targets pulsed with HP53, although HP53 stimulated CTL showed cross-reactive lysis against P18-pulsed target cells. Cross-reactivity was also shown in immunization in vivo and with target cells endogenously expressing viral protein in vitro using two different recombinant vaccinia viruses expressing only the N-terminal portion of gp160, containing P18 but not HP53. Peptide cross-contamination was excluded. Cold target inhibition and single cell cloning experiments indicated that the same CTL was responding to both peptides. Using substituted and truncated peptides, we explored amino acid residues critical for cross-reactive CTL recognition, identified fine specificity similarities among all cross-reactive CTL lines but not non-cross-reactive lines, and mapped cross-reactivity to a 10-residue core of P18 and to an eight-residue core of HP53. A comparison of these peptide sequences and recent data on residues of P18 interacting with H-2Dd provided us with clues to residues involved in the interaction of the CTL with the MHC-peptide complex.

Keywords: Amino Acid Sequence Animal Cross Reactions Human HIV Envelope Protein gp160/CHEMISTRY/*IMMUNOLOGY/METABOLISM Immunodominant Epitopes/CHEMISTRY/*METABOLISM Mice Mice, Inbred BALB C Mice, Inbred Strains Molecular Sequence Data Peptide Fragments/CHEMISTRY/*IMMUNOLOGY/METABOLISM Sequence Analysis T-Lymphocytes, Cytotoxic/*IMMUNOLOGY JOURNAL ARTICLE
970228
M9721862

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