Surface-expressed phosphoglycerate mutase of Candida albicans binds to salivary DMBT1

Oho, Takahiko; Setoguchi, Daisuke; Nagata, Emi

doi:10.1007/s00203-023-03605-w

Cited by 1 publication

(2 citation statements)

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“…This protein has also been described in C. albicans cell surface and it is capable of binding to plasminogen, FH , and the salivary agglutinin gp-340, important for oral microbial adherence . This protein has also been related to the virulence of the yeast, and showed the lowest homology among all the organisms tested, with values of 23% and 52% for A.…”

Section: Discussionmentioning

confidence: 99%

“… 58 This protein has also been described in C. albicans cell surface and it is capable of binding to plasminogen, FH 55 , 59 and the salivary agglutinin gp-340, important for oral microbial adherence. 60 This protein has also been related to the virulence of the yeast, 61 and showed the lowest homology among all the organisms tested, with values of 23% and 52% for A. fumigatus and human homologue proteins, respectively. This could be of special interest, as it could be a potential target for diagnostic or treatment options since the chances of side effects or cross-reactivity would be lower.…”

Section: Discussionmentioning

confidence: 99%

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Identification of the Most Immunoreactive Antigens of Candida auris to IgGs from Systemic Infections in Mice

Areitio,

Antoran,

Rodriguez-Erenaga

et al. 2024

J. Proteome Res.

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The delay in making a correct diagnosis of Candida auris causes concern in the healthcare system setting, and immunoproteomics studies are important to identify immunoreactive proteins for new diagnostic strategies. In this study, immunocompetent murine systemic infections caused by non-aggregative and aggregative phenotypes of C. auris and by Candida albicans and Candida haemulonii were carried out, and the obtained sera were used to study their immunoreactivity against C. auris proteins. The results showed higher virulence, in terms of infection signs, weight loss, and histopathological damage, of the non-aggregative isolate. Moreover, C. auris was less virulent than C. albicans but more than C. haemulonii. Regarding the immunoproteomics study, 13 spots recognized by sera from mice infected with both C. auris phenotypes and analyzed by mass spectrometry corresponded to enolase, phosphoglycerate kinase, glyceraldehyde-3phosphate dehydrogenase, and phosphoglycerate mutase. These four proteins were also recognized by sera obtained from human patients with disseminated C. auris infection but not by sera obtained from mice infected with C. albicans or Aspergillus fumigatus. Spot identification data are available via ProteomeXchange with the identifier PXD049077. In conclusion, this study showed that the identified proteins could be potential candidates to be studied as new diagnostic or even therapeutic targets for C. auris.

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