Structure of equine infectious anemia virus matrix protein.

Journal article

The Gag polyprotein is key to the budding of retroviruses from host cells and is cleaved upon virion maturation, the N-terminal membrane-binding domain forming the matrix protein (MA). The 2.8-A resolution crystal structure of MA of equine infectious anemia virus (EIAV), a lentivirus, reveals that, despite showing no sequence similarity, more than half of the molecule can be superimposed on the MAs of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV). However, unlike the structures formed by HIV-1 and SIV MAs, the oligomerization state observed is not trimeric. We discuss the potential of this molecule for membrane binding in the light of conformational differences between EIAV MA and HIV or SIV MA.

Authors: Hatanaka, H; Iourin, O; Rao, Z; Fry, E; Kingsman, A

• Publication status: Published
• Journal: Journal of virology
• Volume: 76
• Issue: 4
• Pages: 1876-1883
• Publication date: 2002-02-01
• DOI: 10.1128/jvi.76.4.1876-1883.2002
• EISSN: 1098-5514
• ISSN: 0022-538X
• Language: English
• Keywords: Crystallization; Molecular Sequence Data; Sequence Alignment; HIV Antigens; Infectious Anemia Virus, Equine; Protein Conformation; Viral Matrix Proteins; Simian immunodeficiency virus; Gene Products, gag; Models, Molecular; Viral Proteins; Crystallography, X-Ray; Amino Acid Sequence; gag Gene Products, Human Immunodeficiency Virus