The structure of avian polyomavirus reveals variably sized capsids, non-conserved inter-capsomere interactions, and a possible location of the minor capsid protein VP4.
Avian polyomavirus (APV) causes a fatal, multi-organ disease among several bird species. Using cryogenic electron microscopy and other biochemical techniques, we investigated the structure of APV and compared it to that of mammalian polyomaviruses, particularly JC polyomavirus and simian virus 40. The structure of the pentameric major capsid protein (VP1) is mostly conserved; however, APV VP1 has a unique, truncated C-terminus that eliminates an intercapsomere-connecting β-hairpin observed in other polyomaviruses. We postulate that the terminal β-hairpin locks other polyomavirus capsids in a stable conformation and that absence of the hairpin leads to the observed capsid size variation in APV. Plug-like density features were observed at the base of the VP1 pentamers, consistent with the known location of minor capsid proteins VP2 and VP3. However, the plug density is more prominent in APV and may include VP4, a minor capsid protein unique to bird polyomaviruses.
Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, USA.
Peter S
PS
Shen
Dirk
D
Enderlein
Christian D S
CD
Nelson
Weston S
WS
Carter
Masaaki
M
Kawano
Li
L
Xing
Robert D
RD
Swenson
Norman H
NH
Olson
Timothy S
TS
Baker
R Holland
RH
Cheng
Walter J
WJ
Atwood
Reimar
R
Johne
David M
DM
Belnap
D000818:Animals; D002213:Capsid / Q000648:ultrastructure*; D036022:Capsid Proteins / Q000378:metabolism* / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D046911:Macromolecular Substances / Q000648:ultrastructure*; D046408:Melopsittacus / Q000821:virology; D011120:Polyomavirus / Q000302:isolation & purification / Q000648:ultrastructure*
D036022:Capsid Proteins; D046911:Macromolecular Substances
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