Molecular characterization of gag proteins from simian immunodeficiency virus (SIVMne)

Henderson, L E; Benveniste, R E; Sowder, R; Copeland, T D; Schultz, Alan M.; Oroszlan, Stephen

doi:10.1128/jvi.62.8.2587-2595.1988

Cited by 177 publications

(67 citation statements)

References 43 publications

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“…Linkage of myristic acid (C14:0) to the N-terminal of a glycine residue found on some viral, cellular, or bacterial proteins, is known as N-terminal myristoylation [120][121][122][123]. Several viral proteins are myristoylated including the poliovirus VP4 protein, simian immunodeficiency virus (SIV) Gag protein, human immunodeficiency virus (HIV) negative regulatory factor (Nef) protein, and the pre-S1 protein of the hepatitis B virus (HBV) [124][125][126][127]. All of these proteins contain the conserved sequence motif 1 MGxxxS/T, where 'x' can be any amino acid [80].…”

Section: Myristoylationmentioning

confidence: 99%

Coronavirus envelope protein: current knowledge

Schoeman

Fielding

2019

Virol J

1,854

1,859

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Background Coronaviruses (CoVs) primarily cause enzootic infections in birds and mammals but, in the last few decades, have shown to be capable of infecting humans as well. The outbreak of severe acute respiratory syndrome (SARS) in 2003 and, more recently, Middle-East respiratory syndrome (MERS) has demonstrated the lethality of CoVs when they cross the species barrier and infect humans. A renewed interest in coronaviral research has led to the discovery of several novel human CoVs and since then much progress has been made in understanding the CoV life cycle. The CoV envelope (E) protein is a small, integral membrane protein involved in several aspects of the virus’ life cycle, such as assembly, budding, envelope formation, and pathogenesis. Recent studies have expanded on its structural motifs and topology, its functions as an ion-channelling viroporin, and its interactions with both other CoV proteins and host cell proteins. Main body This review aims to establish the current knowledge on CoV E by highlighting the recent progress that has been made and comparing it to previous knowledge. It also compares E to other viral proteins of a similar nature to speculate the relevance of these new findings. Good progress has been made but much still remains unknown and this review has identified some gaps in the current knowledge and made suggestions for consideration in future research. Conclusions The most progress has been made on SARS-CoV E, highlighting specific structural requirements for its functions in the CoV life cycle as well as mechanisms behind its pathogenesis. Data shows that E is involved in critical aspects of the viral life cycle and that CoVs lacking E make promising vaccine candidates. The high mortality rate of certain CoVs, along with their ease of transmission, underpins the need for more research into CoV molecular biology which can aid in the production of effective anti-coronaviral agents for both human CoVs and enzootic CoVs.

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Section: Myristoylationmentioning

confidence: 99%

Coronavirus envelope protein: current knowledge

Schoeman

Fielding

2019

Virol J

1,854

1,859

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“…Design of protease inhibitors that might serve as drugs against AIDS is greatly facilitated by a detailed understanding of the structure and function of this enzyme. Part of this understanding has been provided by studies of the substrate specificity of the proteases from both types 1 and 2 HIV (Darke et al, 1988;Henderson et al, 1988;Konvalinka et al, 1990;Margolin et al, 1990;Phylip et al, 1990;Tozser et al, 1991;Griffiths et al, 1992). Our laboratory has evaluated a wide variety of nonviral proteins as substrates for the HIV proteases Tomasselli et al, 1990aTomasselli et al, , 1991a and, together with data from other laboratories (e.g., Shoeman et al, 1991;Tomaszek et al, 1992) has compiled an extensive database of octapeptide sequences from known substrates.…”

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confidence: 99%

Human immunodeficiency virus type‐1 reverse transcriptase and ribonuclease h as substrates of the viral protease

Tomasselli¹,

Sarcich²,

Barrett³

et al. 1993

Protein Science

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A study has been made of the susceptibility of recombinant constructs of reverse transcriptase (RT) and ribonuclease H (RNase H) from human immunodeficiency virus type 1 (HIV-1) to digestion by the HIV-1 protease. At neutral pH, the protease attacks a single peptide bond, Phe440-Tyr441, in one of the protomers of the folded, active RT/RNase H (p66/p66) homodimer to give a stable, active heterodimer (~6 6 1~5 1 ) that is resistant to further hydrolysis (Chattopadhyay, D., et al., 1992, J. Biol. Chem. 267, 14227-14232). The COOH-terminal p15 fragment released in the process, however, is rapidly degraded by the protease by cleavage at Tyr,,,-Leu,,, and Leu,,,. In marked contrast to this p15 segment, both p66/p51 and a folded RNase H construct are stable to breakdown by the protease at neutral pH. It is only at pH values around 4 that these latter proteins appear to unfold and, under these conditions, the heterodimer undergoes extensive proteolysis. RNase H is also hydrolyzed at low pH, but cleavage takes place primarily at Gly,,,-Ala,,, and at Phe440-Tyr441, and only much more slowly at residues 483,494, and 532. This observation can be reconciled by inspection of crystallographic models of RNase H, which show that residues 483,494, and 532 are relatively inaccessible in comparison to Gly,,, and Phe,,. Our results fit a model in which the p66/p66 homodimer exists in a conformation that mirrors that of the heterodimer, but with a plS segment on one of the protomers that is structurally disordered to the extent that all of its potential HIV protease cleavage sites are accessible for hydrolysis.

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“…Originally NC proteins were purified from RV virions (Davis et al, 1976;Henderson et al, 1981Henderson et al, , 1988Henderson et al, , 1990Henderson et al, , 1992Hizi et al, 1987;Prats et al, 1988Prats et al, , 1990 and later from recombinant Escherichia coli or synthesized in vitro by chemical methods (see below) and found to bind a wide variety of nucleic acids (NA) molecules with a preference for the genomic 70S RNA (Darlix and Spahr, 1985;Wu et al, 1996). Accordingly, the relative affinity of in vitro synthesized NC protein for retroviral RNA, DNA and oligonucleotides is in the order 'retroviral RNA > ssDNA > dsDNA > oligonucleotides' where the apparent affinity constant for the genomic RNA is 5 × 10 7 M −1 , about 25 times higher than that for poly(rA) (You and McHenry, 1993).…”

Section: Large Scale Synthesis Of Rv Nc Proteins and Zinc Bindingmentioning

confidence: 99%

Retrospective on the all-in-one retroviral nucleocapsid protein

et al. 2014

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This review aims at briefly presenting a retrospect on the retroviral nucleocapsid protein (NC), from an unspecific nucleic acid binding protein (NABP) to an all-in-one viral protein with multiple key functions in the early and late phases of the retrovirus replication cycle, notably reverse transcription of the genomic RNA and viral DNA integration into the host genome, and selection of the genomic RNA together with the initial steps of virus morphogenesis. In this context we will discuss the notion that NC protein has a flexible conformation and is thus a member of the growing family of intrinsically disordered proteins (IDPs) where disorder may account, at least in part, for its function as a nucleic acid (NA) chaperone and possibly as a protein chaperone vis-à-vis the viral DNA polymerase during reverse transcription. Lastly, we will briefly review the development of new anti-retroviral/AIDS compounds targeting HIV-1 NC because it represents an ideal target due to its multiple roles in the early and late phases of virus replication and its high degree of conservation.

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Molecular characterization of gag proteins from simian immunodeficiency virus (SIVMne)

Cited by 177 publications

References 43 publications

Coronavirus envelope protein: current knowledge

Coronavirus envelope protein: current knowledge

Human immunodeficiency virus type‐1 reverse transcriptase and ribonuclease h as substrates of the viral protease

Retrospective on the all-in-one retroviral nucleocapsid protein

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