4.4 Review

LysM proteins in mammalian fungal pathogens

Journal

FUNGAL BIOLOGY REVIEWS
Volume 40, Issue -, Pages 114-122

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.fbr.2022.02.001

Keywords

LysM; Fungi; Effector; Chitinase; Mammalian pathogen; Fungal virulence

Categories

Funding

  1. Spanish National Research Plan [RTI2018-099371-B-I00]

Ask authors/readers for more resources

LysM domain is a highly conserved carbohydrate-binding module that recognizes polysaccharides containing N-acetylglucosamine residues, found in a wide variety of extracellular proteins and receptors. Limited studies have focused on the expression and roles of LysM proteins in mammalian fungal pathogens, leaving a gap in knowledge and research.
The LysM domain is a highly conserved carbohydrate-binding module that recognizes polysaccharides containing N-acetylglucosamine residues. LysM domains are found in a wide variety of extracellular proteins and receptors from viruses, bacteria, fungi, plants and animals. LysM proteins are also present in many species of mammalian fungal pathogens, although a limited number of studies have focused on the expression and determination of their putative roles in the infection process. This review summarizes the current knowledge and recent studies on LysM proteins in the main morphological groups of fungal pathogens that cause infections in humans and other mammals. Recent advances towards understanding the biological functions of LysM proteins in infections of mammalian hosts and their use as potential targets in antifungal strategies are also discussed. (c) 2022 The Author(s). Published by Elsevier Ltd on behalf of British Mycological Society. This is an open access article under the CC BY license (http://creativecommons.org/

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available