scholarly journals Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid

1991 ◽  
Vol 266 (22) ◽  
pp. 14539-14547
Author(s):  
S.C. Pettit ◽  
J. Simsic ◽  
D.D. Loeb ◽  
L. Everitt ◽  
C.A. Hutchison ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cleavage Sites ◽  
Structural Requirements ◽  
Protease Cleavage ◽  
Protease Cleavage Sites ◽  
Retroviral Protease

scholarly journals Ty1 Proteolytic Cleavage Sites Are Required for Transposition: All Sites Are Not Created Equal

2001 ◽  
Vol 75 (2) ◽  
pp. 638-644 ◽  
Author(s):  
Gennady V. Merkulov ◽  
Joseph F. Lawler ◽  
Yolanda Eby ◽  
Jef D. Boeke
Keyword(s):  
Virus Assembly ◽  
The Other ◽  
Cleavage Sites ◽  
Protease Cleavage ◽  
Sequence Of Events ◽  
Key Enzyme ◽  
Protease Cleavage Sites ◽  
Proteolytic Cleavages ◽  
Retroviral Protease

ABSTRACT The retroviral protease is a key enzyme in a viral multienzyme complex that initiates an ordered sequence of events leading to virus assembly and propagation. Viral peptides are initially synthesized as polyprotein precursors; these precursors undergo a number of proteolytic cleavages executed by the protease in a specific and presumably ordered manner. To determine the role of individual protease cleavage sites in Ty1, a retrotransposon from Saccharomyces cerevisiae, the cleavage sites were systematically mutagenized. Altering the cleavage sites of the yeast Ty1 retrotransposon produces mutants with distinct retrotransposition phenotypes. Blocking the Gag/PR site also blocks cleavage at the other two cleavage sites, PR/IN and IN/RT. In contrast, mutational block of the PR/IN or IN/RT sites does not prevent cleavage at the other two sites. Retrotransposons with mutations in each of these sites have transposition defects. Mutations in the PR/IN and IN/RT sites, but not in the Gag/PR site, can be complemented in trans by endogenous Ty1 copies. Hence, the digestion of the Gag/PR site and release of the protease N terminus is a prerequisite for processing at the remaining sites; cleavage of PR/IN is not required for the cleavage of IN/RT, and vice versa. Of the three cleavage sites in the Gag-Pol precursor, the Gag/PR site is processed first. Thus, Ty1 Gag-Pol processing proceeds by an ordered pathway.

scholarly journals A novel HIV vaccine targeting the protease cleavage sites

2017 ◽  
Vol 14 (1) ◽  
Author(s):  
Hongzhao Li ◽  
Robert W. Omange ◽  
Francis A. Plummer ◽  
Ma Luo
Keyword(s):  
Hiv Vaccine ◽  
Cleavage Sites ◽  
Protease Cleavage ◽  
Protease Cleavage Sites

scholarly journals Proteolytic Cleavage of Bovine Adenovirus 3-Encoded pVIII

2017 ◽  
Vol 91 (10) ◽  
Author(s):  
Amit Gaba ◽  
Lisanework Ayalew ◽  
Niraj Makadiya ◽  
Suresh Tikoo
Keyword(s):  
Cleavage Site ◽  
Virus Assembly ◽  
Proteolytic Cleavage ◽  
Efficient Production ◽  
Cleavage Sites ◽  
Bovine Adenovirus ◽  
Protease Cleavage Site ◽  
Protease Cleavage ◽  
Protease Cleavage Sites ◽  
Single Protease

ABSTRACT Proteolytic maturation involving cleavage of one nonstructural and six structural precursor proteins including pVIII by adenovirus protease is an important aspect of the adenovirus life cycle. The pVIII encoded by bovine adenovirus 3 (BAdV-3) is a protein of 216 amino acids and contains two potential protease cleavage sites. Here, we report that BAdV-3 pVIII is cleaved by adenovirus protease at both potential consensus protease cleavage sites. Usage of at least one cleavage site appears essential for the production of progeny BAdV-3 virions as glycine-to-alanine mutation of both protease cleavage sites appears lethal for the production of progeny virions. However, mutation of a single protease cleavage site of BAdV-3 pVIII significantly affects the efficient production of infectious progeny virions. Further analysis revealed no significant defect in endosome escape, genome replication, capsid formation, and virus assembly. Interestingly, cleavage of pVIII at both potential cleavage sites appears essential for the production of stable BAdV-3 virions as BAdV-3 expressing pVIII containing a glycine-to-alanine mutation of either of the potential cleavage sites is thermolabile, and this mutation leads to the production of noninfectious virions. IMPORTANCE Here, we demonstrated that the BAdV-3 adenovirus protease cleaves BAdV-3 pVIII at both potential protease cleavage sites. Although cleavage of pVIII at one of the two adenoviral protease cleavage sites is required for the production of progeny virions, the mutation of a single cleavage site of pVIII affects the efficient production of infectious progeny virions. Further analysis indicated that the mutation of a single protease cleavage site (glycine to alanine) of pVIII produces thermolabile virions, which leads to the production of noninfectious virions with disrupted capsids. We thus provide evidence about the requirement of proteolytic cleavage of pVIII for production of infectious progeny virions. We feel that our study has significantly advanced the understanding of the requirement of adenovirus protease cleavage of pVIII.

scholarly journals Identification of the protease cleavage sites in a reconstituted Gag polyprotein of an HERV-K(HML-2) element

Retrovirology ◽  
2011 ◽  
Vol 8 (1) ◽  
pp. 30 ◽  
Author(s):  
Maja George ◽  
Torsten Schwecke ◽  
Nadine Beimforde ◽  
Oliver Hohn ◽  
Claudia Chudak ◽  
...  
Keyword(s):  
Cleavage Sites ◽  
Gag Polyprotein ◽  
Protease Cleavage ◽  
Protease Cleavage Sites

scholarly journals Regulating ENaC’s gate

2020 ◽  
Vol 318 (1) ◽  
pp. C150-C162 ◽  
Author(s):  
Thomas R. Kleyman ◽  
Douglas C. Eaton
Keyword(s):  
Cleavage Sites ◽  
Open Probability ◽  
Protease Cleavage ◽  
Inositol Phospholipids ◽  
Human Disorders ◽  
Protease Cleavage Sites ◽  
Specific Factors ◽  
The Impact ◽  
Channel Transition ◽  
Extracellular Environment

Epithelial Na+ channels (ENaCs) are members of a family of cation channels that function as sensors of the extracellular environment. ENaCs are activated by specific proteases in the biosynthetic pathway and at the cell surface and remove embedded inhibitory tracts, which allows channels to transition to higher open-probability states. Resolved structures of ENaC and an acid-sensing ion channel revealed highly organized extracellular regions. Within the periphery of ENaC subunits are unique domains formed by antiparallel β-strands containing the inhibitory tracts and protease cleavage sites. ENaCs are inhibited by Na+ binding to specific extracellular site(s), which promotes channel transition to a lower open-probability state. Specific inositol phospholipids and channel modification by Cys-palmitoylation enhance channel open probability. How these regulatory factors interact in a concerted manner to influence channel open probability is an important question that has not been resolved. These various factors are reviewed, and the impact of specific factors on human disorders is discussed.

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