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Published on: March 11, 2022
Protein-O-mannosyltransferases in virulence and development
K B Lengeler1, D Tielker, J F Ernst
1Institut für Mikrobiologie, Molekulare Mykologie, Heinrich-Heine-Universität Düsseldorf, Universitätsstr. 1/26.12, 40225, Düsseldorf, Germany.
Cellular and Molecular Life Sciences : CMLS
|November 3, 2007
Summary
Protein-O-mannosyltransferases (Pmt proteins) add mannose to proteins, impacting cell walls, differentiation, and virulence in fungi, bacteria, and mammals. This review explores Pmt roles in development and disease.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Protein-O-mannosyltransferases (Pmt proteins) catalyze O-mannosylation, a crucial post-translational modification.
- This modification is conserved across diverse organisms, including fungi, mammals, insects, and bacteria.
- O-mannosylation plays vital roles in cell wall integrity, differentiation, and virulence.
Purpose of the Study:
- To review the diverse functions of Pmt proteins.
- To highlight the involvement of Pmt proteins in cellular differentiation, development, and virulence.
- To discuss the implications of O-mannosylation in human diseases and pathogen virulence.
Main Methods:
- Literature review of studies on Protein-O-mannosyltransferases.
- Analysis of the roles of O-mannosylation in various organisms.
- Examination of Pmt protein involvement in disease pathogenesis.
Main Results:
- O-mannosylation is essential for fungal cell wall structure, differentiation, and virulence.
- Pmt proteins are critical for mammalian and insect development; deficiencies cause muscular dystrophy.
- O-mannosylation influences the virulence of Candida albicans and Mycobacterium tuberculosis.
Conclusions:
- Pmt proteins are key regulators of fundamental biological processes across species.
- Dysregulation of O-mannosylation is linked to human diseases and pathogen virulence.
- Further research into Pmt proteins could yield therapeutic strategies for infectious diseases and developmental disorders.
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