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Leaky Scanning

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R...

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Related Experiment Video

Updated: May 9, 2025

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit

Published on: June 28, 2013

Exploring TMPRSS2 Drug Target to Combat Influenza and Coronavirus Infection.

Krishnaprasad Baby¹, Megh Pravin Vithalkar¹, Somasish Ghosh Dastidar²

¹Department of Pharmacology, Manipal College of Pharmaceutical Sciences, Manipal Academy of Higher Education, Manipal, Karnataka 576104, India.

|April 29, 2025

Summary

This summary is machine-generated.

Transmembrane serine protease 2 (TMPRSS2) is crucial for respiratory virus entry and spread. Inhibiting TMPRSS2 offers a promising strategy to develop new antiviral therapies against influenza and coronaviruses.

Keywords:

COVID-19 treatment SARS-CoV-2 antiviral therapy coronavirus host proteases influenza virus protease inhibition public health strategies tTMPRSS2 viral pathogenesis

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Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein

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Area of Science:

Virology
Molecular Biology
Pathogenesis

Background:

Respiratory viral infections like influenza and COVID-19 pose global health threats.
Transmembrane serine protease 2 (TMPRSS2) is a host cell protease vital for viral entry and pathogenesis.
TMPRSS2 activates viral surface proteins, facilitating cell entry and spread of viruses such as SARS-CoV-2 and influenza.

Purpose of the Study:

To review the critical role of TMPRSS2 in viral replication and pathogenicity.
To explore TMPRSS2 as a therapeutic target for novel antiviral agents.
To highlight strategies for developing targeted TMPRSS2 inhibitors.

Main Methods:

Literature review of studies on TMPRSS2 function in viral infections.
Analysis of TMPRSS2's role in activating viral proteins (e.g., SARS-CoV-2 spike protein, influenza hemagglutinin).
Examination of the impact of TMPRSS2 inhibition on viral spread and disease severity.

Main Results:

TMPRSS2 facilitates viral entry by cleaving viral glycoproteins, enabling membrane fusion.
Coexpression of TMPRSS2 with ACE2 receptors in the respiratory tract is key for SARS-CoV-2 infection.
TMPRSS2 activation of hemagglutinin is essential for influenza virus spread.
Inhibiting TMPRSS2 can reduce viral propagation, inflammation, and disease severity.

Conclusions:

TMPRSS2 is a significant factor in the pathogenesis of major respiratory viruses.
Targeting TMPRSS2 presents a viable therapeutic strategy for developing broad-spectrum antiviral drugs.
Further research into TMPRSS2 inhibitors could lead to improved public health outcomes for viral respiratory infections.