The papillomavirus major capsid protein L1. Buck, C. B., Day, P. M., & Trus, B. L. 445(1):169–174. doi abstract bibtex The elegant icosahedral surface of the papillomavirus virion is formed by a single protein called L1. Recombinant L1 proteins can spontaneously self-assemble into a highly immunogenic structure that closely mimics the natural surface of native papillomavirus virions. This has served as the basis for two highly successful vaccines against cancer-causing human papillomaviruses (HPVs). During the viral life cycle, the capsid must undergo a variety of conformational changes, allowing key functions including the encapsidation of the ~8 kb viral genomic DNA, maturation into a more stable state to survive transit between hosts, mediating attachment to new host cells, and finally releasing the viral DNA into the newly infected host cell. This brief review focuses on conserved sequence and structural features that underlie the functions of this remarkable protein.
@article{buck_papillomavirus_2013,
title = {The papillomavirus major capsid protein L1},
volume = {445},
issn = {1096-0341},
doi = {10.1016/j.virol.2013.05.038},
abstract = {The elegant icosahedral surface of the papillomavirus virion is formed by a single protein called L1. Recombinant L1 proteins can spontaneously self-assemble into a highly immunogenic structure that closely mimics the natural surface of native papillomavirus virions. This has served as the basis for two highly successful vaccines against cancer-causing human papillomaviruses ({HPVs}). During the viral life cycle, the capsid must undergo a variety of conformational changes, allowing key functions including the encapsidation of the {\textasciitilde}8 kb viral genomic {DNA}, maturation into a more stable state to survive transit between hosts, mediating attachment to new host cells, and finally releasing the viral {DNA} into the newly infected host cell. This brief review focuses on conserved sequence and structural features that underlie the functions of this remarkable protein.},
pages = {169--174},
number = {1},
journaltitle = {Virology},
shortjournal = {Virology},
author = {Buck, Christopher B. and Day, Patricia M. and Trus, Benes L.},
date = {2013-10},
pmid = {23800545},
pmcid = {PMC3783536},
keywords = {{HPV}, Humans, Papillomaviridae, Human papillomavirus 16, Amino Acid Sequence, Capsid Proteins, Conserved Sequence, Genes, Viral, Heparan Sulfate Proteoglycans, {HPV}16, L2, Maturation, Oncogene Proteins, Viral, Protein Folding, Protein Interaction Mapping, Virion, Virus Assembly, Virus Internalization},
file = {Plný text:C\:\\Users\\Miroslava Kuderavá\\Zotero\\storage\\B3NUG39F\\Buck et al. - 2013 - The papillomavirus major capsid protein L1.pdf:application/pdf},
}
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During the viral life cycle, the capsid must undergo a variety of conformational changes, allowing key functions including the encapsidation of the ~8 kb viral genomic DNA, maturation into a more stable state to survive transit between hosts, mediating attachment to new host cells, and finally releasing the viral DNA into the newly infected host cell. 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