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dc.contributor.authorBista, Sandhya
dc.contributor.authorSingh, Preeti
dc.contributor.authorBernard, Quentin
dc.contributor.authorYang, Xiuli
dc.contributor.authorHart, Thomas
dc.contributor.authorLin, Yi Pin
dc.contributor.authorKitsou, Chrysoula
dc.contributor.authorSingh Rana, Vipin
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorZhnag, Kai
dc.contributor.authorAkins, Darrin R.
dc.contributor.authorHritzo, Lucy
dc.contributor.authorKim, Yuri
dc.contributor.authorGrab, Dennis J.
dc.contributor.authorDumler, J. Stephen
dc.contributor.authorPal, Utpal
dc.date2020
dc.date.accessioned2022-06-27T15:41:32Z
dc.date.available2022-06-27T15:41:32Z
dc.date.issued2020-04-07
dc.identifier.citationA novel laminin-binding protein mediates microbial-endothelial cell interactions and facilitates dissemination of Lyme disease pathogens, S. Bista, P. Singh, Q. Bernard, X. Yang, T. Hart, Y.-P. Lin, C. Kitsou, V. S. Rana, F. Zhang, R. J. Linhardt, K. Zhang, D. R. Akins, L. Hritzo, Y. Kim, D. J. Grab, J. S. Dumler, U. Pal, Journal of Infectious Diseases, 221, 1438–1447, 2020.
dc.identifier.issn15376613
dc.identifier.issn221899
dc.identifier.urihttps://doi.org/10.1093/infdis/jiz626
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5506
dc.descriptionJournal of Infectious Diseases, 221, 1438–1447
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.abstractBorrelia burgdorferi conserved gene products BB0406 and BB0405, members of a common B. burgdorferi paralogous gene family, share 59% similarity. Although both gene products can function as potential porins, only BB0405 is essential for infection. Here we show that, despite sequence homology and coexpression from the same operon, both proteins differ in their membrane localization attributes, antibody accessibility, and immunogenicity in mice. BB0406 is required for spirochete survival in mammalian hosts, particularly for the disseminated infection in distant organs. We identified that BB0406 interacts with laminin, one of the major constituents of the vascular basement membrane, and facilitates spirochete transmigration across host endothelial cell barriers. A better understanding of how B. burgdorferi transmigrates through dermal and tissue vascular barriers and establishes disseminated infections will contribute to the development of novel therapeutics to combat early infection.
dc.description.sponsorshipNational Science Foundation
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofJournal of Infectious Diseases
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleA novel laminin-binding protein mediates microbial-endothelial cell interactions and facilitates dissemination of Lyme disease pathogens
dc.typeArticle
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1093/infdis/jiz626
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)
rpi.description.pages1438-1447
rpi.description.volume221


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