Virus-host interactions in African swine fever: the attachment to cellular receptors

Abstract

Biochemical and morphological techniques have shown that African swine fever virus (ASFV) enters susceptible cells by a mechanism of receptor-mediated endocytosis. The virus binds to a specific, saturable site in the cell and this interaction is required for a productive infection. A structural ASFV protein of 12kDa (p12) has been identified to be involved in the recognition of the cellular receptor, on the basis of the specific binding of the polypeptide to sensitive Vero cells. Protein p12 is externally located in the virus particle, forming disulfide-linked dimers with an apparent molecular mass of 17kDa. The gene has been mapped within the central region of the BA71V strain genome. Sequencing analysis has shown the existence of an open reading frame encoding a polypeptide of 61 amino acids characterized by the presence of a putative transmembrane domain, and a cysteine rich region in the C-terminal part which may be responsible for the dimerization of the protein. Transcripts of the p12 gene were only synthesized during the late phase of the infectious cycle. No posttranslational modifications of the polypeptide, such as glycosylation, phosphorylation or fatty acid acylation, have been found. The comparison of the amino acid sequence of protein p12 from 11 different virus strains has revealed a high degree of conservation of the polypeptide.