BST-2 mediated restriction of simian-human immunodeficiency virus

Autor: John C. Guatelli, Autumn Ruiz, Richard S. Mitchell, David Lau, Kimberly Schmitt, Edward B. Stephens, M. Sarah Hill
Rok vydání: 2010
Předmět:
animal diseases
viruses
Human Immunodeficiency Virus Proteins
Simian Acquired Immunodeficiency Syndrome
HIV Infections
medicine.disease_cause
Gene Products
nef
Transmembrane domain
Rhesus macaque
Viral Regulatory and Accessory Proteins
Immunodeficiency
0303 health sciences
Membrane Glycoproteins
Pig-tailed macaque
030302 biochemistry & molecular biology
BST-2
virus diseases
Virus Release
Transmembrane protein
3. Good health
SHIV
Simian Immunodeficiency Virus
Macaca nemestrina
Reassortant Viruses
Molecular Sequence Data
Biology
GPI-Linked Proteins
Article
Cell Line
03 medical and health sciences
Antigens
CD
Virology
Vpu
medicine
Animals
Humans
Amino Acid Sequence
Simian–human immunodeficiency virus
030304 developmental biology
Simian immunodeficiency virus
medicine.disease
Macaca mulatta
Protein tertiary structure
Protein Structure
Tertiary
Virus release
Tetherin
HIV-1
Sequence Alignment
Zdroj: Virology. 406(2)
ISSN: 1096-0341
Popis: Pathogenic simian–human immunodeficiency viruses (SHIV) contain HIV-1 Vpu and SIV Nef, both shown to counteract BST-2 (HM1.24; CD317; tetherin) inhibition of virus release in a species-specific manner. We show that human and pig-tailed BST-2 (ptBST-2) restrict SHIV. We found that sequential “humanization” of the transmembrane domain (TMD) of the pig-tailed BST-2 (ptBST-2) protein resulted in a fluctuation in sensitivity to HIV-1 Vpu. Our results also show that the length of the TMD in human and ptBST-2 proteins is important for BST-2 restriction and susceptibility to Vpu. Taken together, our results emphasize the importance of tertiary structure in BST-2 antagonism and suggests that the HIV-1 Vpu transmembrane domain may have additional functions in vivo unrelated to BST-2 antagonism.
Databáze: OpenAIRE
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