Cystatin and cystatin-derived peptides have antibacterial activity against the pathogen Porphyromonas gingivalis.
We investigated whether cystatins and cystatin-derived peptides, encompassing sequences of secondary structures of cystatin S and papain binding domains of cystatin C, display antimicrobial properties. Of the different microorganisms tested, only the growth of P. gingivalis was inhibited by chicken cystatin and cystatin C. Cystatin S, cystatin S:1-14, cystatin S:61-73 and cystatin S:108-121 also inhibited its growth, whereas cystatin S:21-38, cystatin S:39-55, cystatin S:81-95, cystatin S:94-109, and cystatin C: 9-12/55-60/106-107 did not. No inhibition of the cysteine proteinase activity of P. gingivalis was observed for all cystatin-derived peptides. On the other hand, leupeptin and antipain inhibited P. gingivalis proteinase activity, but had no effect on the growth. These data suggest that cystatins contain antibacterial sequences active against P. gingivalis and that the growth inhibition does not depend on the inhibition of P. gingivalis cysteine proteinases.
Blankenvoorde
M F
MF
Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), The Netherlands.
van't Hof
W
W
Walgreen-Weterings
E
E
van Steenbergen
T J
TJ
Brand
H S
HS
Veerman
E C
EC
Nieuw Amerongen
A V
AV
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D015891:Cystatins / Q000737:chemistry / Q000494:pharmacology*; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology*; D016966:Porphyromonas gingivalis / Q000187:drug effects* / Q000254:growth & development; D017433:Protein Structure, Secondary
D000900:Anti-Bacterial Agents; D015891:Cystatins; D010455:Peptides