INTRODUCTION: Human metapneumovirus (hMPV), initially described in 2001, is an enveloped RNA virus of the genus Metapneumovirus, subfamily Pneumovirinae, family Paramyxoviridae.
OBJECTIVE: We sought to clarify the basic features of hMPV proteins.
METHODS: Rabbits were immunized with inactivated virions of hMPV Chinese isolate, CHN05-01, to yield anti-hMPV antiserum. Antiserum was used as primary antibody to detect hMPV proteins by Western blotting. NetNglyc 1.0 server, NetOglyc 3.1 server, and the NetPhos 2.0 server were applied for predicting potential glycosylation and phosphorylation sites of proteins of prototype virus of subtype A, CAN97-83.
RESULTS: The highest reactive titer of the antiserum with hMPV antigens reached 1:500 in enzyme-linked immunosorbent assay. Potential glycosylation sites of G protein and phosphorylation sites of P protein were greatest among all hMPV proteins. G protein was shown as a narrow band with molecular weight between 55 and 72 kd (∼68 kd), indicating that its glycosylation level is consistent and remarkably different from that of CAN99-80 and CAN99-81. F1 subunit of fusion protein displayed molecular weight between 40 and 55 kd (∼48 kd), which is consistent with previous reports.
CONCLUSIONS: Basic features of 2 major membrane proteins of Chinese hMPV isolate were clarified, which will benefit future studies on protein function and the pathogenesis of this virus.
Submitted by Xiaodong Zhao
- Copyright © 2008 by the American Academy of Pediatrics