Cell-binding properties of the envelope proteins of porcine endogenous retroviruses.

To examine the binding properties of the envelope glycoproteins of porcine endogenous retrovirus subgroups A and B (PERV-A and PERV-B), we produced two forms of soluble envelope proteins, termed Env-ST and Env-SU, using a baculovirus expression system. Env-ST and Env-SU encompass one-third of the N-terminal and the entire surface unit (SU) of the envelope protein, respectively. Using these proteins, binding assays were performed in various mammalian cell lines. The binding properties of the Env-STs that contain the putative receptor binding domain (RBD) did not correlate with the susceptibility to the pseudotype viruses having PERV envelopes, whereas those of the Env-SUs correlated fairly well. These results suggested that the Env-SUs but not Env-STs interacted with their receptors in various cell lines. Interestingly, PERV-A Env-SU did not bind to a mink cell line (Mv1-Lu cells) that is highly susceptible to the PERV-A pseudotype virus. In addition, PERV-B Env-SU did not interfere with the PERV-B pseudotype virus on Mv1-Lu cells. These results suggest the existence of a cognate receptor-independent entry pathway as demonstrated in an immunodeficiency-inducing variant of feline leukemia virus FeLV.