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A host-derived pent...
A host-derived pentapeptide enhancing host-bacteria commensalisms and communication
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- Drobni, Mirva (författare)
- Umeå universitet,Kariologi
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- Li, Tong (författare)
- Umeå universitet,Kariologi
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Krüger, Karina (författare)
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- Loimaranta, Vuokko (författare)
- Umeå universitet,Kariologi
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Kilian, Mogens (författare)
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Hammarström, Lennart (författare)
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Jörnvall, Hans (författare)
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Bergman, Tomas (författare)
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- Strömberg, Nicklas (författare)
- Umeå universitet,Kariologi
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(creator_code:org_t)
- Washington : American society for microbiology, 2006
- 2006
- Engelska.
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Ingår i: Infection and Immunity. - Washington : American society for microbiology. - 0019-9567 .- 1098-5522. ; 74:11, s. 6293-6299
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Salivary proline-rich proteins (PRPs) attach commensal Actinomyces and Streptococcus species to teeth. Here, gel filtration, mass spectrometry and Edman degradation were applied to show the release of a pentapeptide, RGRPQ, from PRP-1 upon proteolysis by Streptococcus gordond. Moreover, synthetic RGRPQ and derivatives were used to investigate associated innate properties and responsible motifs. The RGRPQ peptide increased 2.5-fold the growth rate of S. gordonii via a Q-dependent sequence motif and selectively stimulated oral colonization of this organism in a rat model in vivo. In contrast, the growth of Streptococcus mutans, implicated in caries, was not affected. While the entire RGRPQ sequence was required to block sucrose-induced pH-decrease by S. gordonii and S. mutans, the N-terminal Arg residue mediated the pH increase (i.e., ammonia production) by S. gordonii alone (which exhibits Arg catabolism to ammonia). Strains of commensal viridans streptococci exhibited PR-P degradation and Arg catabolism, whereas cariogenic species did not. The RGRPQ peptide mediated via a differential Q-dependent sequence motif, adhesion inhibition, and desorption of PRP-1-binding strains of A. naeslundii genospecies 2 (5 of 10 strains) but not of S. gordonii (n = 5). The inhibitable A. naeslundii strains alone displayed the same binding profile as S. gordond to hybrid peptides terminating in RGRPQ or GQSPQ, derived from the middle or C-terminal segments of PRP-1. The present findings indicate the presence of a host-bacterium interaction in which a host peptide released by bacterial proteolysis affects key properties in biofilm formation.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Immunology in the medical area (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Infektionsmedicin (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Infectious Medicine (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Odontologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Dentistry (hsv//eng)
Nyckelord
- proline-rich proteins
- candida albicans
- oral bacteria
- salivary agglutinin
- apatitic surfaces
- innate immunity
- Dental caries
- Gordonii
- commensal
- statherin
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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