scholarly journals BAR-encapsulated nanoparticles for the inhibition and disruption of Porphyromonas gingivalis–Streptococcus gordonii biofilms

2018 ◽  
Vol 16 (1) ◽  
Author(s):  
Mohamed Y. Mahmoud ◽  
Donald R. Demuth ◽  
Jill M. Steinbach-Rankins
Microbiology ◽  
1994 ◽  
Vol 140 (4) ◽  
pp. 867-872 ◽  
Author(s):  
R. J. Lamont ◽  
S. Gil ◽  
D. R. Demuth ◽  
D. Malamud ◽  
B. Rosan

1994 ◽  
Vol 17 (5) ◽  
pp. 355-360 ◽  
Author(s):  
Richard J Lamont ◽  
Grace W Hsiao ◽  
Sucheol Gil

2006 ◽  
Vol 60 (1) ◽  
pp. 121-139 ◽  
Author(s):  
Masae Kuboniwa ◽  
Gena D. Tribble ◽  
Chloe E. James ◽  
Ali O. Kilic ◽  
Lin Tao ◽  
...  

PLoS ONE ◽  
2011 ◽  
Vol 6 (11) ◽  
pp. e27386 ◽  
Author(s):  
Juhi Bagaitkar ◽  
Carlo A. Daep ◽  
Carol K. Patel ◽  
Diane E. Renaud ◽  
Donald R. Demuth ◽  
...  

Microbiology ◽  
2002 ◽  
Vol 148 (6) ◽  
pp. 1627-1636 ◽  
Author(s):  
Richard J. Lamont ◽  
Azza El-Sabaeny ◽  
Yoonsuk Park ◽  
Guy S. Cook ◽  
J. William Costerton ◽  
...  

2005 ◽  
Vol 73 (7) ◽  
pp. 3983-3989 ◽  
Author(s):  
Yoonsuk Park ◽  
M. Regina Simionato ◽  
Kachiko Sekiya ◽  
Yukitaka Murakami ◽  
Deanna James ◽  
...  

ABSTRACT Porphyromonas gingivalis, one of the causative agents of adult periodontitis, attaches and forms biofilms on substrata of Streptococcus gordonii. Coadhesion and biofilm development between these organisms requires the interaction of the short fimbriae of P. gingivalis with the SspB streptococcal surface polypeptide. In this study we investigated the structure and binding activities of the short fimbriae of P. gingivalis. Electron microscopy showed that isolated short fimbriae have an average length of 103 nm and exhibit a helical structure with a pitch of ca. 27 nm. Mfa1, the major protein subunit of the short fimbriae, bound to SspB protein, and this reaction was inhibited by purified recombinant Mfa1 and monospecifc anti-Mfa1 serum in a dose-dependent manner. Complementation of a polar Mfa1 mutant with the mfa1 gene restored the coadhesion phenotype of P. gingivalis. Hence, the Mfa1 structural fimbrial subunit does not require accessory proteins for binding to SspB. Furthermore, the interaction of Mfa1 with SspB is necessary for optimal coadhesion between P. gingivalis and S. gordonii.


2020 ◽  
Vol 21 (11) ◽  
pp. 4150 ◽  
Author(s):  
Paulina Ślęzak ◽  
Michał Śmiga ◽  
John W. Smalley ◽  
Klaudia Siemińska ◽  
Teresa Olczak

The oral cavity of healthy individuals is inhabited by commensals, with species of Streptococcus being the most abundant and prevalent in sites not affected by periodontal diseases. The development of chronic periodontitis is linked with the environmental shift in the oral microbiome, leading to the domination of periodontopathogens. Structure-function studies showed that Streptococcus gordonii employs a “moonlighting” protein glyceraldehyde-3-phosphate dehydrogenase (SgGAPDH) to bind heme, thus forming a heme reservoir for exchange with other proteins. Secreted or surface-associated SgGAPDH coordinates Fe(III)heme using His43. Hemophore-like heme-binding proteins of Porphyromonas gingivalis (HmuY), Prevotella intermedia (PinO) and Tannerella forsythia (Tfo) sequester heme complexed to SgGAPDH. Co-culturing of P. gingivalis with S. gordonii results in increased hmuY gene expression, indicating that HmuY might be required for efficient inter-bacterial interactions. In contrast to the ΔhmuY mutant strain, the wild type strain acquires heme and forms deeper biofilm structures on blood agar plates pre-grown with S. gordonii. Therefore, our novel paradigm of heme acquisition used by P. gingivalis appears to extend to co-infections with other oral bacteria and offers a mechanism for the ability of periodontopathogens to obtain sufficient heme in the host environment. Importantly, P. gingivalis is advantaged in terms of acquiring heme, which is vital for its growth survival and virulence.


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