2017
DOI: 10.1128/iai.00774-16
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Streptococcus oralis Neuraminidase Modulates Adherence to Multiple Carbohydrates on Platelets

Abstract: Adherence to host surfaces is often mediated by bacterial binding to surface carbohydrates. Although it is widely appreciated that some bacterial species express glycosidases, previous studies have not considered whether bacteria bind to multiple carbohydrates within host glycans as they are modified by bacterial glycosidases. Streptococcus oralis is a leading cause of subacute infective endocarditis. Binding to platelets is a critical step in disease; however, the mechanisms utilized by S. oralis remain large… Show more

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Cited by 32 publications
(80 citation statements)
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“…Among them, GspB and Hsa are serine-rich repeat glycoproteins (Srr) that bind to sialylated glycans present on the soluble human salivary mucin MG2/MUC7, a component of the mucosal pellicle (64), and the platelet glycoprotein GPIb (65, 66). Srr proteins are important for biofilm formation and have been identified in many other oral streptococci, including Fap1 of S. parasanguinis (67) and S.oralis (68), SrpA of S. sanguinis (69) and S. cristatus (70), and SrpA, B and C of S. salivarius (71). Interestingly, Srr homologs are not present in the caries pathogen S. mutans .…”
Section: Mechanisms Of Colonizationmentioning
confidence: 99%
“…Among them, GspB and Hsa are serine-rich repeat glycoproteins (Srr) that bind to sialylated glycans present on the soluble human salivary mucin MG2/MUC7, a component of the mucosal pellicle (64), and the platelet glycoprotein GPIb (65, 66). Srr proteins are important for biofilm formation and have been identified in many other oral streptococci, including Fap1 of S. parasanguinis (67) and S.oralis (68), SrpA of S. sanguinis (69) and S. cristatus (70), and SrpA, B and C of S. salivarius (71). Interestingly, Srr homologs are not present in the caries pathogen S. mutans .…”
Section: Mechanisms Of Colonizationmentioning
confidence: 99%
“…Given that other SRRPs are associated with fibrils on the bacterial surface, we named these open reading frames fapA (13,992 bp), fapB (13,692 bp), and fapC (15,144 bp), where fap represents fibril-associated protein. Each of these open reading frames is predicted to encode the previously described characteristics of SRRPs, including an atypical N-terminal signal sequence, two serinerich repeat domains that flank the nonrepeat region, and a cell wall anchor domain (2,6,20,21,(36)(37)(38)(39)(40)(41). The atypical signal sequence of SRRPs is approximately 90 amino acids long and is required for secretion via the accessory Sec system (39).…”
Section: Resultsmentioning
confidence: 99%
“…It should be noted that all three predicted SRRPs are distinct from Fap1, the previously characterized S. oralis subsp. oralis SRRP (2).…”
Section: Resultsmentioning
confidence: 99%
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