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dc.contributor.authorMiddleton, D.R.
dc.contributor.authorZhang, X.
dc.contributor.authorWantuch, P.L.
dc.contributor.authorOzdilek, A.
dc.contributor.authorLiu, X.
dc.contributor.authorLopilato, R.
dc.contributor.authorGangasani, N.
dc.contributor.authorBridger, R.
dc.contributor.authorWells, L.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorAvci, F.Y.
dc.date2018
dc.date.accessioned2022-06-27T15:52:26Z
dc.date.available2022-06-27T15:52:26Z
dc.date.issued2018
dc.identifier.citationIdentification of the Streptococcus pneumoniae type 3 capsule-specific glycosyl hydrolase gene of Paenibacillus sp. 32352, D. R. Middleton, X. Zhang, P. L. Wantuch, A. Ozdilek, X. Liu, R. Lopilato, N. Gangasani, R. Bridger, L. Wells, R. J. Linhardt, F. Y. Avci, Glycobiology, 28, 90–99, 2018.
dc.identifier.urihttps://doi.org/10.1093/glycob/cwx097
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5600
dc.descriptionGlycobiology, 28, 90–99
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractBacillus circulans Jordan 32352 was isolated from decaying organic matter in the New Jersey soil in the early 1930s. This soil-dwelling bacterium produced an enzyme capable of degrading the type 3 capsular polysaccharide (Pn3P) of Streptococcus pneumoniae (Spn). Early reports of this enzyme, Pn3Pase, demonstrated its inducibility by, and specificity for Pn3P. We set out to identify and clone this enzyme for its recombinant expression and characterization. We first sequenced the genome of this bacterial species, and reclassified the Pn3Pase producing bacterium as Paenibacillus species 32352. We identified the putative protein of Pn3Pase through mass spectrometry-based proteomics and cloned the gene for recombinant expression. We then characterized the oligosaccharide products generated upon the enzymatic depolymerization of Pn3P. Sequence analysis suggests that this glycoside hydrolase belongs to a new carbohydrate-active enzyme GH family. To our knowledge, this is the only enzyme to demonstrate Pn3P depolymerization activity.
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleIdentification of the Streptococcus pneumoniae type 3 capsule-specific glycosyl hydrolase gene of Paenibacillus sp. 32352
dc.typeArticle
dcterms.isVersionOfhttps://doi.org/10.1093/glycob/cwx097
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)


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