Retrovirology | |
Identification of the protease cleavage sites in a reconstituted Gag polyprotein of an HERV-K(HML-2) element | |
关键词: HERV-K(HML-2); Gag processing; maturation; retrovirus; retroviral protease; endogenous retrovirus; | |
DOI : 10.1186/1742-4690-8-30 | |
来源: DOAJ |
【 摘 要 】
Abstract
Background
The human genome harbors several largely preserved HERV-K(HML-2) elements. Although this retroviral family comes closest of all known HERVs to producing replication competent virions, mutations acquired during their chromosomal residence have rendered them incapable of expressing infectious particles. This also holds true for the HERV-K113 element that has conserved open reading frames (ORFs) for all its proteins in addition to a functional LTR promoter. Uncertainty concerning the localization and impact of post-insertional mutations has greatly hampered the functional characterization of these ancient retroviruses and their proteins. However, analogous to other betaretroviruses, it is known that HERV-K(HML-2) virions undergo a maturation process during or shortly after release from the host cell. During this process, the subdomains of the Gag polyproteins are released by proteolytic cleavage, although the nature of the mature HERV-K(HML-2) Gag proteins and the exact position of the cleavage sites have until now remained unknown.
Results
By aligning the amino acid sequences encoded by the
Conclusions
Expression of reconstituted sequences of original HERV elements is an important tool for studying fundamental aspects of the biology of these ancient viruses. The analysis of HERV-K(HML-2) Gag processing and the nature of the mature Gag proteins presented here will facilitate further studies of the discrete functions of these proteins and of their potential impact on the human host.
【 授权许可】
Unknown