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
ISSN1096-0341
AutoresMario 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
ResumoWe 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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