Abstract:
:The papillomavirus major late protein, L1, forms the pentameric assembly unit of the viral shell. Recombinant HPV16 L1 pentamers assemble in vitro into capsid-like structures, and truncation of ten N-terminal residues leads to a homogeneous preparation of 12-pentamer, icosahedral particles. X-ray crystallographic analysis of these particles at 3.5 A resolution shows that L1 closely resembles VP1 from polyomaviruses. Surface loops contain the sites of sequence variation among HPV types and the locations of dominant neutralizing epitopes. The ease with which small virus-like particles may be obtained from L1 expressed in E. coli makes them attractive candidate components of a papillomavirus vaccine. Their crystal structure also provides a starting point for future vaccine design.
journal_name
Mol Celljournal_title
Molecular cellauthors
Chen XS,Garcea RL,Goldberg I,Casini G,Harrison SCdoi
10.1016/s1097-2765(00)80449-9subject
Has Abstractpub_date
2000-03-01 00:00:00pages
557-67issue
3eissn
1097-2765issn
1097-4164pii
S1097-2765(00)80449-9journal_volume
5pub_type
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