The proteolytic potential of Candida albicans in human saliva supplemented with glucose

Samaranayake, LP; Hughes, Anne E.; MacFarlane, T. W.

doi:10.1099/00222615-17-1-13

Cited by 63 publications

(36 citation statements)

References 27 publications

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“…Wall lytic enzymes may also be required for germ tube formation (Ram et al, 1984;Sullivan et al, 1984). Recent reports on proteases secreted by C. albicans (MacDonald, 1984;Samaranayake et al, 1984;Ruchel, 1984) have all emphasized their possible roles in the pathogenicity of C. albicans, but have not considered the possibility that the breakdown of cytoplasmic materials or wall glycoproteins may also be integrally involved in germ tube formation. We have yet to show a relationship between ethanol and mobilization of carbohydrate or nitrogen reserves in C. albicans, yet it would seem very likely that such mobilization is necessary for germ tube formation to occur.…”

Section: J H P O L L a C K A N D T Hashimoto Discussionmentioning

confidence: 99%

Ethanol-induced Germ Tube Formation in Candida albicans

Pollack¹,

Hashimoto²

1985

Microbiology

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Section: J H P O L L a C K A N D T Hashimoto Discussionmentioning

confidence: 99%

Ethanol-induced Germ Tube Formation in Candida albicans

Pollack¹,

Hashimoto²

1985

Microbiology

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“…Enzyme production is induced in minimal media containing proteins as sole nitrogen source but not by low molecular mass nitrogen sources (Crandall & Edwards, 1987;Ross et al, 1990;Shimizu et al, 1987). In addition, glucose stimulates its production (Samaranayake et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

Detection of intracellular forms of secretory aspartic proteinase in Candida albicans

Homma¹,

Kanbe²,

Chibana³

et al. 1992

Journal of General Microbiology

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The extracellular proteinase (EPR) of Ctadidiz d b~~ was induced in a medium containing bovine serum albumin as sole nitrogen source. There were two intracellular forms in cells induced to produce EPR, a 43 kDa protein (EPR) and a 45kDa protein (cross-reacting material of EPR; CRM-EPR); these were detected by h d o t t h g Using anti-EPR antiserum. The 43 kDa protein (EPR) may be the same as the extracellular form judging by molecular mass, a d the 45 kDa protein (CRM-EPR) may be a precursor form of EPR. Many dense granules were observed by electron microscopy near the plasma membrane of the mother cells in EPR-producing cells. Both the 43 and 45 kDa proteins were recovered in a membrane fraction and were solubilized by Triton X-100. When the membrane fraction was further fractionated by sucrose d d t y gradient centrifugation, the 43 and 45 kDa proteins were differentially fractionated. This suggests that they were located in Merent membranebound structures and is consistent with an assumption that the 45 kDa protein is a preclvsor for EPR.

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“…One reason for this may be the salivary buffering action which neutralises the yeastderived carboxylic acids that have rapidly accumulated during the log phase of yeast growth. It is known that acid production in yeast-salivary cultures peaks at the log phase of growth and declines or abates thereafter [17,23]. An acidic pH is crucial for proteinase expression in Candida spp.…”

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confidence: 99%