Taxonomic group: fungi / Mucoromycota
(Phylum: Mucoromycota)
Organ / tissue: cell wall
Publication DOI: 10.1021/bk-2012-1102.ch008Journal NLM ID: 100961485Publisher: American Chemical Society
Correspondence: zomer
galectintherapeutics.com
Institutions: Pro-Pharmaceuticals, Newton, USA
A heat stable complex polysaccharide (molecular weight of 4300 Da) purified from the cell wall of the fungus Mucor rouxii (CPM) and a cationic polysaccharide from crab chitin (CPP) are potent antifungal agents both in vitro and in vivo. These compounds possess several highly desirable characteristics for the next generation of antifungal agents. First, being novel compounds, unrelated to the existing antifungal drugs, there is no cross resistance between the compounds and the currently used antifungal agents. Second is the importance of the rapidity of action, low MIC (Minimum Inhibitory Concentration) values and the lethal effect of these compounds against a wide spectrum of pathogenic yeasts. This will help reduce treatment duration and the development of untoward effects. Third, these compounds are heat and light-stable, making them promising to use for topical applications as was proven by the in vivo experiments with CPP. Fourth, being a large molecule with highly charged residues, these compounds are acting on external targets of the cell membrane. Thus, it is unlikely to develop resistance to CPM by the efflux mechanism that is a major cause of drug resistance in microorganisms including fungi.
cytology, Mucor rouxii, antifungal agents, cell membranes, candidiasis
Structure type: structural motif or average structure ; 4300
Location inside paper: Scheme 1, CPM
Trivial name: polyglucosamine
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85
Methods: biological assays
Biological activity: CPM is potent antifungal agents against Candida albicans and non-albicans Candida species both in vitro and in vivo; plasma membrane interacts with CPM and affects the action of the proton translocating ATPase pump (H+ -ATPase)
NCBI Taxonomy refs (TaxIDs): 29923Reference(s) to other database(s): GTC:G97099AY
Show glycosyltransferases
There is only one chemically distinct structure:
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(later renamed to: Amylomyces rouxii)