The Rosen laboratory focuses on understanding interactions between bacteria and human neutrophils. Recent emphasis has been on using the bacterial response to neutrophil phagocytosis (mRNA expression profiles) to reflect bacterial prioritization of the multifactorial threats to microbial survival within the neutrophil phagosome. Upregulated genes are used to identify systems that may be important for microbial survival under these conditions. Targeted gene deletions are the used to evaluate the importance of the gene products for microbial survival in neutrophils and virulence in a murine infection model. Dr. Rosen collaborates with Dr. Klebanoff.
Rosen H, Crowley JR and Heinecke JW . Human neutrophils use the myeloperoxidase-hydrogen peroxide-chloride system to chlorinate but not nitrate bacterial proteins during phagocytosis. J Biol Chem 2002; 277:30463-8
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Staudinger BJ, Oberdoerster MA, Lewis PJ and Rosen H. mRNA expression profiles for Escherichia coli ingested by normal and phagocyte oxidase-deficient human neutrophils. J Clin Invest 2002; 110:1151-63
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Rosen H. Bacterial responses to neutrophil phagocytosis. Curr Opin Hematol 2004; 11:1-6
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Rosen H, Lewis PJ and Nitzel CM. Neutrophil microbicidal activity: screening bacterial mutants for survival after phagocytosis using quantitative PCR. Jpn J Infect Dis 2004; 57:S19-21
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Navarre W, Porwollik S, Wang Y, McClelland M, Rosen H, Libby S, Fang F. Selective Silencing of Foreign DNA with Low GC Content by the H-NS Protein in Salmonella. Science 2006; 1-7, 313:236-8
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Amory J, Rosen H, Sukut C, Wallace F, Saints S. Clinical problem-solving. A jaundiced eye. N. Engl. J. Med. 2006; 354:1516-1520
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Johnson JR, Clabots C, Rosen H. Effect of inactivation of the global oxidative stress regulator oxyR on the colonization ability of Escherichia coli O1:K1:H7 in a mouse model of ascending urinary tract infection. Infect. Immun. 2006; 74:461-468
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Wang Y, Rosen H, Madtes DK, Shao B, Martin TR, Heinecke JW, Fu X. Myeloperoxidase inactivates TIMP-1 by oxidizing its N-terminal cysteine residue: An oxidative mechanism for regulating proteolysis during inflammation. J. Biol. Chem. 2007; 282:31826-31834
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