Mubashshir Rasheed

ORCID: 0000-0002-1597-6976
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About
Contact & Profiles
Research Areas
  • Antifungal resistance and susceptibility
  • Fungal Infections and Studies
  • Pneumocystis jirovecii pneumonia detection and treatment
  • Peptidase Inhibition and Analysis
  • Fungal Biology and Applications
  • Fungal and yeast genetics research

Centre for DNA Fingerprinting and Diagnostics
2013-2022

Manipal Academy of Higher Education
2018

A family of 11 GPI (glycosylphosphatidylinositol)-linked cell surface-associated aspartyl proteases (yapsins) in the human opportunistic fungal pathogen Candida glabrata is required for wall remodelling, pH homoeostasis, survival macrophages and virulence a murine model disseminated candidiasis. In present paper, we report new roles yapsins C. physiology implicate them first time regulation vacuole homoeostasis. study show that mutant lacking all yapsins, Cgyps1-11∆, possesses an enlarged...

10.1042/bj20130757 article EN Biochemical Journal 2013-12-18

Secretory proteins are key modulators of host–pathogen interaction. The human opportunistic fungal pathogen Candida glabrata lacks secreted proteolytic activity but possesses 11 glycosylphosphatidylinositol-anchored aspartyl proteases, also referred to as Yapsins (CgYps1–11), that essential for its virulence. To delineate the role CgYapsins in interaction with host cells, we have profiled, through liquid chromatography-tandem mass spectrometry (LC-MS/MS) approach, total secretome wild-type...

10.1021/acs.jproteome.9b00299 article EN publisher-specific-oa Journal of Proteome Research 2019-10-17

Invasive candidiasis poses a major healthcare threat. The human opportunistic fungal pathogen Candida glabrata, which causes mucosal and deep-seated infections, is armed with distinct virulence attributes, including family of 11 glycosylphosphatidylinositol-linked aspartyl proteases, CgYapsins. Here, we have profiled total membrane proteomes the C. glabrata wildtype proteases-deficient strain, Cgyps1-11Δ, by mass spectrometry analysis uncovered novel role for yapsins in glucose sensing...

10.1016/j.jbc.2022.101593 article EN cc-by Journal of Biological Chemistry 2022-01-17
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