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Amino Acid Changes at Positions 173 and 187 in the Human T-Cell Leukemia Virus Type 1 Surface Glycoprotein Induce Specific Neutralizing Antibodies

By Sophie Blanchard, Thérèse Astier-Gin, Béatrice Tallet, Daniel Moynet, Danielle Londos-Gagliardi and Bernard Guillemain


The nucleotide sequence of human T-cell leukemia virus type 1 (HTLV-1) is highly conserved, most strains sharing at least 95% sequence identity. This sequence conservation is also found in the viral env gene, which codes for the two envelope glycoproteins that play a major role in the induction of a protective immune response against the virus. However, recent reports have indicated that some variations in env sequences may induce incomplete cross-reactivity between HTLV-1 strains. To identify the amino acid changes that might be involved in the antigenicity of neutralizable epitopes, we constructed expression vectors coding for the envelope glycoproteins of two HTLV-1 isolates (2060 and 2072) which induced human antibodies with different neutralization patterns. The amino acid sequences of the envelope glycoproteins differed at four positions. Vectors coding for chimeric or point-mutated envelope proteins were derived from 2060 and 2072 HTLV-1 env genes. Syncytium formation induced by the wild-type or mutated envelope proteins was inhibited by human sera with different neutralizing specificities. We thus identified two amino acid changes, I173→V and A187→T, that play an important role in the antigenicity of neutralizable epitopes located in this region of the surface envelope glycoprotein

Topics: Pathogenesis and Immunity
Publisher: American Society for Microbiology
Year: 1999
OAI identifier:
Provided by: PubMed Central
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