This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Trichomonad parasites, T. vaginalis (Tv) and T. foetus (Tf), cause major sexually transmitted diseases in human and cattle, respectively, and may predispose human patients to AIDS infection. BNS et al. purified lipophosphoglycan from both parasites an treated them with mild acid (trifluoroacetic acid) and different enzymes (endo-beta-galactosidase, another beta-galactosidase, phospholipase C) in order to obtain oligosaccharide structures short enough for MS/MS characterization. The fractions from Tv were initially characterized by MALDI-TOF MS, then the oligosaccharide portions were reduced and permethylated before analysis by LC-MS/MS, using a graphite column and a QoTOF mass spectrometer. or the LTQ-Orbitrap MS system. A variety of sugars assigned to different structural motifs was identified. Many structures have been assigned and further data interpretation and investigation is ongoing. Biological characterization has shown that the T. vaginalis Lipophosphoglycan triggers a selective upregulation of cytokines by human female reproductive tract epithelial cells. Two manuscripts describing results from this project have been published recently and a poster was presented at the 2009 International Mass Spectrometry Conference in Bremen, Germany.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR010888-14
Application #
8170911
Study Section
Special Emphasis Panel (ZRG1-BCMB-H (40))
Project Start
2010-06-01
Project End
2011-05-31
Budget Start
2010-06-01
Budget End
2011-05-31
Support Year
14
Fiscal Year
2010
Total Cost
$10,197
Indirect Cost
Name
Boston University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
604483045
City
Boston
State
MA
Country
United States
Zip Code
02118
Lu, Yanyan; Jiang, Yan; Prokaeva, Tatiana et al. (2017) Oxidative Post-Translational Modifications of an Amyloidogenic Immunoglobulin Light Chain Protein. Int J Mass Spectrom 416:71-79
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Yu, Xiang; Sargaeva, Nadezda P; Thompson, Christopher J et al. (2015) In-Source Decay Characterization of Isoaspartate and ?-Peptides. Int J Mass Spectrom 390:101-109
Steinhorn, Benjamin S; Loscalzo, Joseph; Michel, Thomas (2015) Nitroglycerin and Nitric Oxide--A Rondo of Themes in Cardiovascular Therapeutics. N Engl J Med 373:277-80

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