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Capsid-Targeted Viral Inactivation: A Novel Tactic for Inhibiting Replication in Viral Infections

View Article: PubMed Central - PubMed

ABSTRACT

Capsid-targeted viral inactivation (CTVI), a conceptually powerful new antiviral strategy, is attracting increasing attention from researchers. Specifically, this strategy is based on fusion between the capsid protein of a virus and a crucial effector molecule, such as a nuclease (e.g., staphylococcal nuclease, Barrase, RNase HI), lipase, protease, or single-chain antibody (scAb). In general, capsid proteins have a major role in viral integration and assembly, and the effector molecule used in CTVI functions to degrade viral DNA/RNA or interfere with proper folding of viral key proteins, thereby affecting the infectivity of progeny viruses. Interestingly, such a capsid–enzyme fusion protein is incorporated into virions during packaging. CTVI is more efficient compared to other antiviral methods, and this approach is promising for antiviral prophylaxis and therapy. This review summarizes the mechanism and utility of CTVI and provides some successful applications of this strategy, with the ultimate goal of widely implementing CTVI in antiviral research.

No MeSH data available.


Gag protein components. The structural protein Gag is mainly processed into four proteins, p17 matrix (MA), p24 capsid (CA), p9 nucleocapsid (NC), and P6, by a virus-encoded protease.
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viruses-08-00258-f002: Gag protein components. The structural protein Gag is mainly processed into four proteins, p17 matrix (MA), p24 capsid (CA), p9 nucleocapsid (NC), and P6, by a virus-encoded protease.

Mentions: Together with HIV-2, HIV-1 originated from the midwestern region of Africa and was transmitted from primates to humans. The viral genome consists of double positive-sense strand RNA, which harbours long terminal repeats (LTRs) at both ends. At least nine proteins, categorized into structural proteins (Gag, Pol, envelope (Env)), regulatory proteins (trans-activator of transcription (Tat), regulator of expression of virion proteins (Rev)), and accessory proteins (virus protein U (Vpu), viral protein R (Vpr), viral infectivity factor (Vif), negative regulatory factor (Nef)), are encoded by the sequence between the LTRs. The Gag gene is translated into a 55 kD protein (pr55), which is processed into p17 matrix (MA), p24 capsid (CA), p9 nucleocapsid (NC), and p6 by a virus-encoded protease (Figure 2). The fusion protein Gag–Pol is generated by ribosomal frameshifting caused by a cis-acting motif in the mRNA [63]. The interior of the capsid contains the genomic RNA, enzymes (reverse transcriptase, integrase [64,65], and protease), as well as host cell components.


Capsid-Targeted Viral Inactivation: A Novel Tactic for Inhibiting Replication in Viral Infections
Gag protein components. The structural protein Gag is mainly processed into four proteins, p17 matrix (MA), p24 capsid (CA), p9 nucleocapsid (NC), and P6, by a virus-encoded protease.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC5035972&req=5

viruses-08-00258-f002: Gag protein components. The structural protein Gag is mainly processed into four proteins, p17 matrix (MA), p24 capsid (CA), p9 nucleocapsid (NC), and P6, by a virus-encoded protease.
Mentions: Together with HIV-2, HIV-1 originated from the midwestern region of Africa and was transmitted from primates to humans. The viral genome consists of double positive-sense strand RNA, which harbours long terminal repeats (LTRs) at both ends. At least nine proteins, categorized into structural proteins (Gag, Pol, envelope (Env)), regulatory proteins (trans-activator of transcription (Tat), regulator of expression of virion proteins (Rev)), and accessory proteins (virus protein U (Vpu), viral protein R (Vpr), viral infectivity factor (Vif), negative regulatory factor (Nef)), are encoded by the sequence between the LTRs. The Gag gene is translated into a 55 kD protein (pr55), which is processed into p17 matrix (MA), p24 capsid (CA), p9 nucleocapsid (NC), and p6 by a virus-encoded protease (Figure 2). The fusion protein Gag–Pol is generated by ribosomal frameshifting caused by a cis-acting motif in the mRNA [63]. The interior of the capsid contains the genomic RNA, enzymes (reverse transcriptase, integrase [64,65], and protease), as well as host cell components.

View Article: PubMed Central - PubMed

ABSTRACT

Capsid-targeted viral inactivation (CTVI), a conceptually powerful new antiviral strategy, is attracting increasing attention from researchers. Specifically, this strategy is based on fusion between the capsid protein of a virus and a crucial effector molecule, such as a nuclease (e.g., staphylococcal nuclease, Barrase, RNase HI), lipase, protease, or single-chain antibody (scAb). In general, capsid proteins have a major role in viral integration and assembly, and the effector molecule used in CTVI functions to degrade viral DNA/RNA or interfere with proper folding of viral key proteins, thereby affecting the infectivity of progeny viruses. Interestingly, such a capsid–enzyme fusion protein is incorporated into virions during packaging. CTVI is more efficient compared to other antiviral methods, and this approach is promising for antiviral prophylaxis and therapy. This review summarizes the mechanism and utility of CTVI and provides some successful applications of this strategy, with the ultimate goal of widely implementing CTVI in antiviral research.

No MeSH data available.