The F-like protein Ac23 enhances the infectivity of the budded virus of gp64-null Autographa californica multinucleocapsid nucleopolyhedrovirus pseudotyped with baculovirus envelope fusion protein F.
The GP64 and F proteins were previously identified as the sole functional envelope fusion proteins in Baculoviridae. F-like proteins, present only in group I nucleopolyhedroviruses (NPVs), are remnant, nonfunctional F proteins. In this report, we describe the effect of the presence or absence of the F-like protein Ac23 in a gp64-null Autographa californica multinucleocapsid NPV pseudotyped with the F protein from Spodoptera exigua multicapsid NPV (SeF). We found that the presence of Ac23 elevates the infectivity of the pseudotyped virus. This is in contrast to the results of Lung et al. (J. Virol. 76:5729-5736, 2002), who found no such effect. The possible reasons for the differing results are discussed.
Wang
Manli
M
Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, People's Republic of China.
Tan
Ying
Y
Yin
Feifei
F
Deng
Fei
F
Vlak
Just M
JM
Hu
Zhihong
Z
Wang
Hualin
H
D000818:Animals; D016367:Baculoviridae / Q000378:metabolism*; D002213:Capsid / Q000737:chemistry; D017353:Gene Deletion; D015967:Gene Expression Regulation, Viral; D016679:Genome, Viral; D008957:Models, Genetic; D017924:Nucleopolyhedroviruses / Q000378:metabolism*; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000737:chemistry; D018411:Spodoptera / Q000821:virology; D014162:Transfection; D014759:Viral Envelope Proteins / Q000737:chemistry*; D014760:Viral Fusion Proteins / Q000737:chemistry*
D011994:Recombinant Proteins; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins