Related Experiment Video

Updated: Jun 7, 2025

Author Spotlight: Enhanced Isolation of Interaction-Null Mutants in Yeast
02:44

Author Spotlight: Enhanced Isolation of Interaction-Null Mutants in Yeast

Published on: December 29, 2023

416

TMPRSS2 in microbial interactions: Insights from HKU1 and TcsH

Zhengyang Pan1,2, Daoqun Li1,2, Leiliang Zhang1,2

  • 1Department of Clinical Laboratory Medicine, The First Affiliated Hospital of Shandong First Medical University & Shandong Provincial Qianfoshan Hospital, Jinan, Shandong, China.

Plos Pathogens
|November 20, 2024
PubMed

Insights

Transmembrane Serine Protease 2 (TMPRSS2) is a key receptor for viruses like HKU1 and bacteria. Its catalytic function is not essential for microbial binding, revealing new therapeutic targets.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Transmembrane Serine Protease 2 (TMPRSS2) is recognized for its protease activity.
  • Emerging evidence identifies TMPRSS2 as a critical host cell receptor for various microbial pathogens.
  • Human coronavirus HKU1 and bacterial exotoxin TcsH utilize TMPRSS2 for cellular entry.

Purpose of the Study:

  • To elucidate the role of TMPRSS2 in microbial interactions beyond its protease function.
  • To investigate the mechanisms of HKU1 and TcsH binding and entry mediated by TMPRSS2.
  • To explore the potential of TMPRSS2 as a therapeutic target for infections and related diseases.

Main Methods:

  • Structural analysis of TMPRSS2-microbe interactions.
  • Biochemical assays to assess TMPRSS2's catalytic activity in microbial binding.
  • Cellular entry studies using viral and bacterial models.

Main Results:

  • HKU1 uses sialoglycan and TMPRSS2 for entry; sialoglycan primes the spike protein for TMPRSS2 binding.
  • TMPRSS2 autocleavage enhances its affinity for the HKU1 spike, promoting viral fusion.
  • TMPRSS2's catalytic activity is dispensable for HKU1 and TcsH interactions, indicating non-proteolytic roles.

Conclusions:

  • TMPRSS2 acts as a crucial receptor for HKU1 and TcsH, with non-catalytic functions vital for pathogenesis.
  • Structural insights into TMPRSS2-microbe interactions offer potential for developing novel therapeutics against viral infections and cancers.
  • Targeting TMPRSS2 interactions presents a promising strategy for combating microbial infections.

More Related Videos

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.2K
Using Microtiter Dish Radiolabeling for Multiple In Vivo Measurements Of Escherichia coli pppGpp Followed by Thin Layer Chromatography06:30

Using Microtiter Dish Radiolabeling for Multiple In Vivo Measurements Of Escherichia coli pppGpp Followed by Thin Layer Chromatography

Published on: June 4, 2019

6.0K

Related Concept Videos

Riboswitches01:56

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
8.1K
Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
3