Artigo Revisado por pares

Individual contributions of the human metapneumovirus F, G, and SH surface glycoproteins to the induction of neutralizing antibodies and protective immunity

2005; Elsevier BV; Volume: 345; Issue: 2 Linguagem: Inglês

10.1016/j.virol.2005.10.016

ISSN

1096-0341

Autores

Mario H. Skiadopoulos, Stéphane Biacchesi, Ursula J. Buchholz, Emérito Amaro-Carambot, Sonja R. Surman, Peter L. Collins, Brian R. Murphy,

Tópico(s)

Parvovirus B19 Infection Studies

Resumo

We evaluated the individual contributions of the three surface glycoproteins of human metapneumovirus (HMPV), namely the fusion F, attachment G, and small hydrophobic SH proteins, to the induction of serum HMPV-binding antibodies, serum HMPV-neutralizing antibodies, and protective immunity. Using reverse genetics, each HMPV protein was expressed individually from an added gene in recombinant human parainfluenza virus type 1 (rHPIV1) and used to infect hamsters once or twice by the intranasal route. The F protein was highly immunogenic and protective, whereas G and SH were only weakly or negligibly immunogenic and protective, respectively. Thus, in contrast to other paramyxoviruses, the HMPV attachment G protein is not a major neutralization or protective antigen. Also, although the SH protein of HMPV is a virion protein that is much larger than its counterparts in previously studied paramyxoviruses, it does not appear to be a significant neutralization or protective antigen.

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