caa a22 4500 378849557 CHVBK 20180305123320.0 cr unu---uuuuu 161128e20030127xx s 000 0 eng 10.1515/BC.2003.020 doi (NATIONALLICENCE)gruyter-10.1515/BC.2003.020 Internalisation and Degradation of Histatin 5 by Candida albicans [Elektronische Daten] [A.L.A. Ruissen, J. Groenink, P. Krijtenberg, E. Walgreen-Weterings, W. van 't Hof, E.C.I. Veerman, A.V. Nieuw Amerongen] 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. Copyright © 2003 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Ruissen A.L.A. aut Groenink J. aut Krijtenberg P. aut Walgreen-Weterings E. aut Hof W. van 't aut Veerman E.C.I. aut Amerongen A.V. Nieuw aut Biological Chemistry Walter de Gruyter 384/1(2003-01-27), 183-190 1431-6730 384:1<183 2003 384 bchm https://doi.org/10.1515/BC.2003.020 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2003.020 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ruissen A.L.A. aut NATIONALLICENCE 700 1- Groenink J. aut NATIONALLICENCE 700 1- Krijtenberg P. aut NATIONALLICENCE 700 1- Walgreen-Weterings E. aut NATIONALLICENCE 700 1- Hof W. van 't aut NATIONALLICENCE 700 1- Veerman E.C.I. aut NATIONALLICENCE 700 1- Amerongen A.V. Nieuw aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 384/1(2003-01-27), 183-190 1431-6730 384:1<183 2003 384 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter