Internalisation and degradation of histatin 5 by Candida albicans
| Autor: | J. Groenink, van 't Hof W, E. Walgreen-Weterings, E.C.I. Veerman, Nieuw Amerongen Av, Krijtenberg P, A.L.A Ruissen |
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| Přispěvatelé: | Orale Biochemie (OUD, ACTA) |
| Rok vydání: | 2003 |
| Předmět: |
Antifungal Agents
Proteolysis Clinical Biochemistry Antimicrobial peptides Molecular Sequence Data Histatins Microbial Sensitivity Tests Cleavage (embryo) Biochemistry Microbiology stomatognathic system Candida albicans Endopeptidases medicine Protease Inhibitors Amino Acid Sequence Salivary Proteins and Peptides Molecular Biology chemistry.chemical_classification biology medicine.diagnostic_test Stereoisomerism biology.organism_classification Yeast Corpus albicans Enzyme chemistry Microscopy Fluorescence Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Histatin Peptides |
| Zdroj: | Biological Chemistry, 384, 183-190. Walter de Gruyter GmbH Biological chemistry, 384, 183-190. De Gruyter Ruissen, A L A, Groenink, J, Krijtenberg, P, Walgreen-Weterings, E, van 't Hof, W, Veerman, E C I & van Nieuw Amerongen, A 2003, ' Internalisation and degradation of histatin 5 by Candida albicans ', Biological Chemistry, vol. 384, pp. 183-190 . https://doi.org/10.1515/BC.2003.020 |
| ISSN: | 1431-6730 |
| DOI: | 10.1515/BC.2003.020 |
| Popis: | Histatins, salivary antimicrobial peptides, are susceptible to proteolytic degradation, often ascribed to host proteinases. In this study, we addressed the question whether proteolytic activity from microbial sources can contribute to this degradation. Candida albicans, an opportunistic yeast that is susceptible to the histatins, was used as target organism. The most potent histatin (histatin 5: sequence: DSHAKRHHGYKRKFHEKHHSHRGY), two histatin 5 fragments (dh-5: sequence: KRKFHEKHHSHRGY; P-113: sequence: AKRHHGYKRKFH) and an all-D isomer of the latter (P-113D) were used as model peptides. All L-peptides were susceptible to degradation by C. albicans. Cleavage was established at Lys5 and His19 of histatin 5, Lys11, Arg12, Phe14, Glu16, Lys17, His18 and Ser20 of dh-5 and Ala4 and Lys11 of P-113. In addition, it was found that secreted C. albicans enzymes are not involved in the degradation process and that blocking cell entry of the peptides greatly impedes degradation. Moreover, P-113D, which is biologically as active as P-113, was hardly susceptible to proteolysis. These data imply that proteolysis occurs mainly intracellularly and is not used as a protective mechanism against histatin activity. Together, our results suggest that, besides host proteinases, microbial enzymes play an important role in histatin degradation. |
| Databáze: | OpenAIRE |
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