Objectives
The Hsa/GspB adhesins of the oral bacterium Streptococcus gordonii are glycoproteins that bind to sialic acid. Hsa/GspB are peptidoglycan-associated proteins that have the Leu-Pro-X-Thr-Gly (LPXTG) motif and they have sialic acid-dependent hemagglutinating (HA) activity. In S. gordonii DL1, Hsa is the only HA factor for human erythrocytes, whereas the clinical isolate, S. gordonii NDU1118, has sialic-acid-dependent HA activity via GspB and distinct sialic-acid-independent HA activity. This study aimed to identify sialic-acid-independent adhesins in S. gordonii NDU1118.
Methods
The complete genome of the NDU1118 strain was sequenced and annotated. LPXTG-containing proteins were identified and compared with those of the DL1 strain to select candidate genes unique to the NDU1118 strain. The candidate genes were individually deleted to construct mutant strains, which were then tested for sialic-acid-independent HA activity in neuraminidase (sialidase)-treated human erythrocytes.
Results
Genome sequencing of S. gordonii NDU1118 identified 31 putative peptidoglycan-associated proteins containing the LPXTG motif. Homology analysis revealed that NDA_1151 and NDA_2061 did not have homologs in the DL1 strain and were therefore selected as potential adhesin candidates. Reverse transcription-PCR confirmed that both genes were transcribed in the NDU1118 strain. Deletion of NDA_1151 or NDA_2061 abolished HA activity in neuraminidase-treated erythrocytes.
Conclusions
NDA_1151 and NDA_2061 encode novel sialic-acid-independent adhesins, designated aggregation of sialidase-treated hematids 1 (ash1) and ash2, respectively.
扫码关注我们
求助内容:
应助结果提醒方式:
