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Yi-Pin Lin, Ph.D.

  • Yi-Pin Lin, Ph.D.

    Yi-Pin Lin, Ph.D.

    • Zoonotic Diseases

    • Ph.D., Cornell University
    • Postdoctoral training: Tufts University School of Medicine

    yi-pin.lin@health.ny.gov
    Office: 518-402-2233; Lab: 518-473-2789

Research Interests

Lyme disease, transmitted by the bacteria Borrelia burgdorferi, is the most common vector-borne disease in the U.S. The bacteria can infect at the site of the tick bite and then survive in the bloodstream and spread to the heart, joints, or brain, resulting arthritis, neurological abnormalities, and carditis. According to the Center of Disease Control and Prevention (CDC), approximate 30,000 people are infected annually, and most of them are in the Mid-west and Northeast states including New York State.

The research in my laboratory investigates the mechanisms of pathogen-host interactions. We are particularly interested in how the Lyme disease bacteria, Borrelia burgdorferi, survive in two distinct host environments (ticks and vertebrate hosts) by escaping from the killing of the complement system to cause transmission between hosts, dissemination, and diseases. Our goal is to identify and analyze the complement- or complement regulator-binding factors of B. burgdorferi, which facilitate the immune evasion, tissue colonization, and bloodstream survival in different hosts. The approach is to use genome-wide screens such as Transposon-sequencing technology (Tn-seq) to identify these factors and then test their contributions to the disease by using biochemical and genetic techniques and murine models. These factors could be targets to block the bacterial transmission between hosts. Illumination of the mechanisms employed by B. burgdorferi to interact with hosts will promote the development of prophylactic and therapeutic approaches to improve human health.

Select Publications

Yang, X., Lin, Y.P., Heselpoth, R.D., Buyuktanjr, O., Qin, J., Kung, F., Nelson, D.C., Leong, J.M., Pal, U.
Middle region of the Borrelia burgdorferi surface-located protein 1 (Lmp1) interacts with host chondroitin-6-sulfate and independently facilitates infection.
Cell. Microbiol.
(2016)
(18):
97-110.
Lin, Y.P., Bhowmick, R., Coburn, J., Leong, J.M.
Host cell heparan sulfate glycosaminoglycans are ligands for OspF-related proteins of the Lyme disease spirochete.
Cell. Microbiol.
(2015)
(17):
1464-1476.
Lin, Y. P., Chen, Q., Ritchie, J., Dufour, N. P., Fisher, J. R., Coburn, J., Leong, J. M.
Glycosaminoglycan binding but not fibronectin binding by Borrelia burgdorferi adhesin BBK32 promotes joint colonization.
Cell. Microbiol.
(2015)
(17):
860-875.
Lin, Y. P., Benoit, V., Yang, X., Martínez-Herranz, R., Pal, U., Leong, J. M.
Strain-specific variation of the decorin-binding adhesin DbpA influences the tissue tropism of the Lyme disease spirochete.
PLoS Pathog.
(2014)
10
e1004238.
Moriarty, T. J., Shi, M., Lin, Y. P., Ebady, R., Zhou, H., Odisho T., Hardy P. O., Diligimen, A. Wu, J., Weening, E., Skare, J., Kubes, P., Leong J. M. Chaconas, G.
Mechanistically distinct steps of B. burgdorferi vascular adhesion under shear force are mediated by BBK32 interactions with host fibronectin and glycosaminoglycans.
Mol. Microbiol.
(2012)
(86):
1116-1131.