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

Journal Article · Mon Feb 20 04:00:00 EST 2006 · Virology

DOI:https://doi.org/10.1016/J.VIROL.2005.1· OSTI ID:20779459

Skiadopoulos, Mario H ^[1]; Biacchesi, Stephane ^[1]; Buchholz, Ursula J ^[1]; Amaro-Carambot, Emerito ^[1]; Surman, Sonja R ^[1]; Collins, Peter L ^[1]; Murphy, Brian R ^[1]

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1. Respiratory Viruses Section, Laboratory of Infectious Diseases, NIAID, NIH, DHHS, Bethesda, MD 20892-8007 (United States)

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.

• OSTI ID: 20779459
• Journal Information: Virology, Journal Name: Virology Journal Issue: 2 Vol. 345; ISSN VIRLAX; ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ANTIBODIES
ANTIGENS
GENES
GENETICS
GLYCOPROTEINS
GTP-ASES
HAMSTERS
IMMUNITY
VIRUSES