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Salivary agglutinin...
Salivary agglutinin, which binds Streptococcus mutans and Helicobacter pylori, is the lung scavenger receptor cysteine-rich protein gp-340.
- Article/chapterEnglish2000
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LIBRIS-ID:oai:gup.ub.gu.se/184270
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https://gup.ub.gu.se/publication/184270URI
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https://doi.org/10.1074/jbc.M006928200DOI
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-8887URI
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
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Salivary agglutinin is a high molecular mass component of human saliva that binds Streptococcus mutans, an oral bacterium implicated in dental caries. To study its protein sequence, we isolated the agglutinin from human parotid saliva. After trypsin digestion, a portion was analyzed by matrix-assisted laser/desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS), which gave the molecular mass of 14 unique peptides. The remainder of the digest was subjected to high performance liquid chromatography, and the separated peptides were analyzed by MALDI-TOF/post-source decay; the spectra gave the sequences of five peptides. The molecular mass and peptide sequence information showed that salivary agglutinin peptides were identical to sequences in lung (lavage) gp-340, a member of the scavenger receptor cysteine-rich protein family. Immunoblotting with antibodies that specifically recognized either lung gp-340 or the agglutinin confirmed that the salivary agglutinin was gp-340. Immunoblotting with an antibody specific to the sialyl Le(x) carbohydrate epitope detected expression on the salivary but not the lung glycoprotein, possible evidence of different glycoforms. The salivary agglutinin also interacted with Helicobacter pylori, implicated in gastritis and peptic ulcer disease, Streptococcus agalactiae, implicated in neonatal meningitis, and several oral commensal streptococci. These results identify the salivary agglutinin as gp-340 and suggest it binds bacteria that are important determinants of either the oral ecology or systemic diseases.
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Xu, Falin
(author)
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Hoang, V M
(author)
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Larsson, Thomas,1947Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry(Swepub:gu)xlarth
(author)
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Bergström, Jörgen,1953Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry(Swepub:gu)xberjo
(author)
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Johansson, IngegerdUmeå universitet,Kariologi(Swepub:umu)injo0003
(author)
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Frängsmyr, L
(author)
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Holmskov, U
(author)
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Leffler, H
(author)
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Nilsson, Carol L,1963Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry(Swepub:gu)xnilca
(author)
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Borén, Thomas
(author)
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Wright, J R
(author)
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Strömberg, NicklasUmeå universitet,Kariologi(Swepub:umu)nist0001
(author)
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Fisher, S J
(author)
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Göteborgs universitetInstitutionen för medicinsk och fysiologisk kemi
(creator_code:org_t)
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In:The Journal of biological chemistry275:51, s. 39860-60021-92581083-351X
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Prakobphol, A
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Xu, Falin
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Hoang, V M
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Larsson, Thomas, ...
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Bergström, Jörge ...
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Johansson, Ingeg ...
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Frängsmyr, L
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Holmskov, U
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Leffler, H
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Nilsson, Carol L ...
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Borén, Thomas
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Wright, J R
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Strömberg, Nickl ...
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Fisher, S J
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University of Gothenburg
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Umeå University