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Cited by 54Glycosylation and Glycoproteins ResearchFungal and yeast genetics researchAntifungal resistance and susceptibility

Biochemical characterization of recombinant Candida albicans mannosyltransferases Mnt1, Mnt2 and Mnt5 reveals new functions in O- and N-mannan biosynthesis

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Díaz-Jiménez, Diana F., Mora-Montes, Héctor M., Hernández-Cervantes, Arturo, Luna-Arias, Juan P., Gow, Neil A.R., Flores-Carreón, Arturo·2012·Biochemical and Biophysical Research Communications
DOI 10.1016/j.bbrc.2012.01.131PMC PMC3480643
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Abstract

The cell surface of Candida albicans is enriched with highly glycosylated mannoproteins that are involved in the interaction with host tissues. N- and O-glycosylation are post-translational modifications that initiate in the endoplasmic reticulum, and finalize in the Golgi. The KRE2/MNT1 family encode a set of multifunctional mannosyltransferases that participate in O-, N- and phosphomannosylation. In order to gain insights into the substrate specificities of these enzymes, recombinant forms of Mnt1, Mnt2, and Mnt5 were expressed in Pichia pastoris and the enzyme activities characterized. Mnt1 and Mnt2 showed a high specificity for α-methylmannoside and α1,2-mannobiose as acceptor substrates. Notably, they also used Saccharomyces cerevisiaeO-mannans as acceptors and generated products with more than three mannose residues, suggesting than Mnt1 and Mnt2 could be the mannosyltransferases adding the fourth and fifth mannose residue to the O-mannans in C. albicans. Mnt5 only recognized α-methylmannoside as acceptor, suggesting that participates in the addition of the second mannose residues to the N-glycan outer chain.

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  • C. auris MNT5 encodes a gene product that decreases cell wall α-mannosylation, resulting in a compensatory increase in cell wall glucan.

    “Like its C. albicans, ortholog C. auris MNT5 also encodes a gene product that decreases cell wall α-mannosylation, perhaps by a decrease in α-1,2 mannan branches, resulting in a compensatory increase in cell wall glucan (16).”

    From Dual function of <i>Candida auris</i> mannosyltransferase, MNT5, in biofilm community protection from antifungal therapy and the host (2025) · cites this paper as [16]

    The Introduction (page unavailable) says C. albicans Mnt5 adds mannose residues to cell-wall mannans, and the Discussion proposes that it adds mannose units to the N-mannan backbone. That is contrary to the sentence’s comparison with a C. albicans gene product that decreases mannosylation. The paper does not examine C. auris or report a compensatory increase in glucan. (LLM, conf=0.84)

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  • Cell wall and extracellular matrix polysaccharides have mechanistic roles implicated in protection of Candida species from host response and drug therapies.

    “Cell wall and extracellular matrix polysaccharides have mechanistic roles implicated in the protection of Candida species from host response and drug therapies (13–16).”

    From Dual function of <i>Candida auris</i> mannosyltransferase, MNT5, in biofilm community protection from antifungal therapy and the host (2025) · cites this paper as [16]

    The Introduction (page unavailable) says C. albicans cell-wall polysaccharides contribute to a protective structure, that mannosylation affects recognition by the host innate immune system, and that disrupting certain mannosyltransferases increases antibiotic sensitivity. It does not address extracellular-matrix polysaccharides or establish protection from host responses and drug therapies across Candida species. (LLM, conf=0.85)

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  • In C. albicans, MNT5 is important for the addition of α-1,2 mannan branches.

    “In C. albicans, MNT5 has been shown to be important for the addition of the α-1,2 mannan branches (16).”

    From Dual function of <i>Candida auris</i> mannosyltransferase, MNT5, in biofilm community protection from antifungal therapy and the host (2025) · cites this paper as [16]

    The Discussion proposes that Mnt5 helps add the second mannose residue to lateral branches of the N-mannan outer chain. However, the Results state that the linkage of Mnt5’s enzymatic product could not be determined, so the paper does not establish the claimed α-1,2 linkage. (LLM, conf=0.86)

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Cites

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Research works printed but not linked: 26

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Authors
Díaz-Jiménez, D. F., Mora-Montes, H. M., Hernández-Cervantes, A., Luna-Arias, J. P., Gow, N. A. R., & Flores-Carreón, A.
Affiliations
  • Universidad de Guanajuato (MX)
  • University of Aberdeen (GB)
Corresponding author
Flores-Carreón, Arturo
ORCID
Gow, Neil A.R.
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2012-03
Volume
419
Issue
1
Pages
77-82
ISSN
0006-291X (ISSN-L)
DOI
10.1016/j.bbrc.2012.01.131
PMC
PMC3480643
OpenAlex
W2117464055
Cited by
54
References
2
Citations by year
2026: 3 · 2025: 3 · 2024: 8 · 2023: 2 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 5 · 2018: 5 · 2017: 5 · 2016: 4 · 2015: 2 · 2014: 6 · 2013: 3 · 2012: 1
FWCI
1.54
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Aberdeen University Research Archive (Aberdeen University) (submittedVersion)
Funders
  • CONACYT
  • de Guanajuato, The Wellcome Trust
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
Keywords
Candida albicans, mannosyltransferase, mannoproteins, substrate specificity, alpha-methyl-D-mannoside, recombinant enzyme characterization
MeSH terms
Candida albicans, Fungal Proteins, Mannans, Mannosyltransferases, Models, Chemical, Recombinant Proteins

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