SwePub
Sök i LIBRIS databas

  Extended search

WFRF:(Areschoug Thomas)
 

Search: WFRF:(Areschoug Thomas) > (2010-2014) > Human Siglec-5 Inhi...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004482naa a2200385 4500
001oai:lup.lub.lu.se:090925b4-6cca-4183-b666-3fa7ea56da6c
003SwePub
008160401s2011 | |||||||||||000 ||eng|
024a https://lup.lub.lu.se/record/21685722 URI
024a https://doi.org/10.1074/jbc.M111.2517282 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
100a Nordström, Theréseu Lund University,Lunds universitet,Avdelningen för medicinsk mikrobiologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Medical Microbiology,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)mikr-tno
2451 0a Human Siglec-5 Inhibitory Receptor and Immunoglobulin A (IgA) Have Separate Binding Sites in Streptococcal {beta} Protein.
264 1c 2011
520 a Sialic acid-binding immunoglobulin-like lectins (Siglecs) are receptors believed to be important for regulation of cellular activation and inflammation. Several pathogenic microbes bind specific Siglecs via sialic acid-containing structures at the microbial surface, interactions that may result in modulation of host responses. Recently, it was shown that the group B Streptococcus (GBS) binds to human Siglec-5 (hSiglec-5), an inhibitory receptor expressed on macrophages and neutrophils, via the IgA-binding surface β protein, providing the first example of a protein/protein interaction between a pathogenic microbe and a Siglec. Here we show that the hSiglec-5-binding part of β resides in the N-terminal half of the protein, which also harbors the previously determined IgA-binding region. We constructed bacterial mutants expressing variants of the β protein with non-overlapping deletions in the N-terminal half of the protein. Using these mutants and recombinant β fragments, we showed that the hSiglec-5-binding site is located in the most N-terminal part of β (B6N region; amino acids 1-152) and that the hSiglec-5- and IgA-binding domains in β are completely separate. We showed with BIAcore(TM) analysis that tandem variants of the hSiglec-5- and IgA-binding domains bind to their respective ligands with high affinity. Finally, we showed that the B6N region, but not the IgA-binding region of β, triggers recruitment of the tyrosine phosphatase SHP-2 to hSiglec-5 in U937 monocytes. Taken together, we have identified and isolated the first microbial non-sialic acid Siglec-binding region that can be used as a tool in studies of the β/hSiglec-5 interaction.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Klinisk medicinx Infektionsmedicin0 (SwePub)302092 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Clinical Medicinex Infectious Medicine0 (SwePub)302092 hsv//eng
650 7a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Mikrobiologi inom det medicinska området0 (SwePub)301092 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Microbiology in the medical area0 (SwePub)301092 hsv//eng
700a Movert, Elinu Lund University,Lunds universitet,Avdelningen för medicinsk mikrobiologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Medical Microbiology,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)med-emt
700a Olin, Andersu Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine4 aut0 (Swepub:lu)medk-ano
700a Ali, Syed R4 aut
700a Nizet, Victor4 aut
700a Varki, Ajit4 aut
700a Areschoug, Thomasu Lund University,Lunds universitet,Avdelningen för medicinsk mikrobiologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Medical Microbiology,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)mmb-tar
710a Avdelningen för medicinsk mikrobiologib Institutionen för laboratoriemedicin4 org
773t Journal of Biological Chemistryg 286:39, s. 33981-33991q 286:39<33981-33991x 1083-351X
856u http://www.ncbi.nlm.nih.gov/pubmed/21795693?dopt=Abstracty FULLTEXT
856u http://dx.doi.org/10.1074/jbc.M111.251728y FULLTEXT
8564 8u https://lup.lub.lu.se/record/2168572
8564 8u https://doi.org/10.1074/jbc.M111.251728

Find in a library

To the university's database

Search outside SwePub

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view