The 1.51-Å structure of the poxvirus L1 protein, a target of potent neutralizing antibodies
AUTOR(ES)
Su, Hua-Poo
FONTE
National Academy of Sciences
RESUMO
Although eradicated from nature more than two decades ago, the threat of smallpox has reemerged because of concerns over its use as a biological weapon. We present the structure of the poxvirus L1 protein, a molecule that is conserved throughout the poxvirus family and is nearly identical in vaccinia virus and in variola virus, which causes smallpox. L1 is a myristoylated envelope protein that is a potent target for neutralizing antibodies and an important component of current experimental vaccines. The L1 structure reveals a hydrophobic cavity located adjacent to its N terminus. The cavity would be capable of shielding the myristate moiety, which is essential for virion assembly. The structure of L1 is a step in the elucidation of molecular mechanisms common to all poxviruses that may stimulate the design of safer vaccines and new antipoxvirus drugs.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=555483Documentos Relacionados
- Human Papillomavirus Type 11 Recombinant L1 Capsomeres Induce Virus-Neutralizing Antibodies
- Identification of Two Cross-Neutralizing Linear Epitopes within the L1 Major Capsid Protein of Human Papillomaviruses
- Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus.
- Trimeric structure for an essential protein in L1 retrotransposition
- Characterization of a Major Neutralizing Epitope on Human Papillomavirus Type 16 L1
