Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site.

Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site. Abstract Text:

The specificities of the proteases of 11 retroviruses were studied using a series of oligopeptides with amino acid substitutions in the P1, P3, and P4 positions of a naturally occurring type 1 cleavage site (Val-Ser-Gln-Asn-Tyr downward arrowPro-Ile-Val-Gln) in human immunodeficiency virus type 1 (HIV-1). Previously, the substrate specificity of the P2 site was studied for the same representative set of retroviral proteases, which included at least one member from each of the seven genera of the family Retroviridae (P. Bagossi, T. Sperka, A. Fehér, J. Kádas, G. Zahuczky, G. Miklóssy, P. Boross, and J. Tözsér, J. Virol. 79:4213-4218, 2005). Our enzyme set comprised the proteases of HIV-1, HIV-2, equine infectious anemia virus, avian myeloblastosis virus (AMV), Mason-Pfizer monkey virus, mouse mammary tumor virus (MMTV), Moloney murine leukemia virus, human T-lymphotropic virus type 1, bovine leukemia virus, walleye dermal sarcoma virus, and human foamy virus. Molecular models were used to interpret the similarities and differences in specificity between these retroviral proteases. The results showed that the retroviral proteases had similar preferences (Phe and Tyr) for the P1 position in this sequence context, but differences were found for the P3 and P4 positions. Importantly, the sizes of the P3 and P4 residues appear to be a major contributor for specificity. The substrate specificities correlated well with the phylogenetic tree of the retroviruses. Furthermore, while the specificities of some enzymes belonging to different genera appeared to be very similar (e.g., those of AMV and MMTV), the specificities of the primate lentiviral proteases substantially differed from that observed for a nonprimate lentiviral protease.

Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site. Publishing Authors By Initials

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of virology

VOLUME: 82

Page Numbers: 10111-7

Journal Abbreviation: J. Virol.

ISSN: 1098-5514

DAY: 13

MONTH: 08

YEAR: 2008

Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 113724

Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site.

AFFILIATION: University of Debrecen, Department of Biochemistry and Molecular Biology, Nagyerdei krt. 98, Debrecen H-4012, Hungary.

Country: United States

AGENCY: United States FIC

GRANT: TW01001

ACRONYM: TW

MEDLINETA: J Virol

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site Related Publications

• Amino Acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site.
• Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases.