Sequence analysis of hemin-binding peptide derived from recombinant hemagglutinin-2 of Porphyromonas gingivalis.
- Author:
Qiu-bo YANG
1
;
Fei-yan YU
;
Sheng-hui YANG
Author Information
- Publication Type:Journal Article
- MeSH: Bacterial Proteins; chemistry; genetics; Hemagglutinins; chemistry; genetics; Porphyromonas gingivalis; genetics; Sequence Analysis, Protein
- From: Chinese Journal of Stomatology 2009;44(9):538-542
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo determine the sequence of the active peptide derived from recombinant hemagglutinin (rHA-2) of Porphyromonas gingivalis (Pg).
METHODSThe HA-2 gene from PgATCC33277 was cloned, expressed in Escherichia coli (Ec) BL21 (DE3), and purified. The purified recombinant protein was evaluated for its ability to bind hemin-linked agarose. The active peptide was subjected to endoproteinase-mediated sequence analysis.
RESULTSThe protein expressed in Ec BL21 (DE3) was identified as PgHA-2 by plasmid sequence analysis, Western blotting, and mass spectrometry. The recombinant protein was confirmed functional by its ability to bind hemin. The sequence of the active peptide of rHA-2 was determined to be DHYAVMISKTGTNAG.
CONCLUSIONSThe availability of sequence of the active peptide of rHA-2 provides a foundation for the development of immunoprophylactic and therapeutic agents against this human pathogen.
