Objective:Human metapneumovirus (hMPV)

initially described in 2001

is an enveloped RNA virus of the genus Metapneumovirus

subfamily Pneumovirinae

family Paramyxoviridae. Here we sought to clarify basic features of human metapneumovirus proteins. Methods:Rabbits were immunized with inactivated virons of hMPV Chinese first isolate

CHN05-01

to yield anti-hMPV antiserum. Antiserum was used as primary antibody to detect hMPV proteins by Western blotting. NetNglyc1.0 server

NetOglyc 3.1server and the NetPhos 2.0 server were applied for predicting potential glycosylation and phosphorylation sites of proteins of prototype virus of type A

CAN97-83. Results:The highest reactive titer of the antiserum with hMPV antigens reached 1:500 in ELISA. Potential glycosylation sites of G protein and phosphorylation sites of P protein were greatest among all hMPV proteins. G protein was shown a narrow band with molecular weight between 55 and 72kDa (approximately 68kDa)

indicating its glycosylation level being consistent and remarkably different from that of CAN99-80 and CAN99-81. F1 subunit of fusion protein displayed molecular weight between 40 and 55kDa (approximately 48 kDa)

which is consistent with previous reports. Conclusion:Basic features of two major membrane proteins of Chinese human metapneumovirus isolate were clarified

which will benefit future studies on protein funtion and pathogenesis of this virus.