Abstract
A 40-kDa outer membrane protein (HBP35) has been molecularly cloned from the periodontal pathogen Porphyromonas gingivalis 381. The predicted amino acid sequence of HBP35 consists of 344 amino acid residues, having a molecular weight of 37,559. In the latest computational analysis, a typical signal peptide was suggested to be present at the amino terminus of the protein. On Western blot analysis using an antibody against recombinant HBP35 (rHBP35), two protein bands were seen in crude extracts of the recombinant Escherichia coli. In addition, a lower molecular weight band was seen in the periplasmic fraction. The partial amino acid sequence of the lower molecular weight HBP35 was N-QELKTSADMKGSFKKNVVLE-C at the amino terminus and corresponded to the 22nd to 41st amino acids of the HBP35 protein. This indicates that there is a cleavage site for the signal peptide between the 21st and the 22nd residues. Immunostaining with the anti-rHBP35 antibody showed that the HBP35 protein was mainly located outside of the P. gingivalis cytoplasm. Taken together, the results suggest that HBP35 passes through the inner membrane after cleavage of the signal peptides at the N-terminal of the protein and is bound to the outer membrane of this bacterium.
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