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Conserved features in papillomavirus and polyomavirus capsids
D M Belnap1, N H Olson, N M Cladel
1Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Journal of Molecular Biology
|June 7, 1996
Summary
Papillomaviruses and polyomaviruses share a conserved T=7 dextro capsid structure, despite differences in size and protein sequences. This structural conservation suggests stable internal capsomere contacts are key.
Area of Science:
- Structural virology
- Molecular biology
- Biophysics
Background:
- Papovavirus family viruses, including papillomaviruses and polyomaviruses, assemble capsids from 72 pentameric capsomeres on a T=7 icosahedral lattice.
- Previous studies indicated differing lattice handedness (left-handed for CRPV, right-handed for others) within this family.
- Papillomavirus capsid structures, like those of BPV-1 and HPV-1, exhibit star-shaped capsomeres and can exist in open or closed forms.
Purpose of the Study:
- To investigate the capsid structure and lattice handedness of Cottontail Rabbit Papillomavirus (CRPV).
- To compare the structural features of papillomaviruses with those of polyomaviruses.
- To elucidate the conserved structural elements within the Papovaviridae family.
Main Methods:
- Cryoelectron microscopy and image reconstruction were employed to determine the CRPV capsid structure.
- Comparative analysis of structural data from CRPV, BPV-1, HPV-1, SV40, and murine polyomavirus.
- Examination of capsomere morphology, lattice arrangement, and intercapsomere interactions.
Main Results:
- The CRPV capsid structure was determined to be T=7 dextro (right-handed), consistent with other examined papillomaviruses.
- Open CRPV capsids showed an increased radius compared to closed forms, with star-shaped capsomeres.
- Papillomavirus capsomeres interact similarly to polyomaviruses, despite differences in size and morphology.
Conclusions:
- Papovavirus capsids exhibit a conserved T=7 dextro structure, characterized by 72 pentameric capsomeres.
- Structural conservation persists despite significant variations in viral capsid protein sequences.
- Stable intra-capsomere contacts and flexible inter-capsomere linkages likely drive the conserved capsid architecture.