Peptidoglycan recognition proteins are a new class of human bactericidal proteins

doi:10.1074/jbc.M511631200

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Papers In Press, published online ahead of print December 14, 2005
J. Biol. Chem, 10.1074/jbc.M511631200
Submitted on October 27, 2005
Revised on December 5, 2005
Accepted on December 13, 2005

Peptidoglycan recognition proteins are a new class of human bactericidal proteins

Xiaofeng Lu, Minhui Wang, Jin Qi, Haitao Wang, Xinna Li, Dipika Gupta, and Roman Dziarski

Indiana University School of Medicine-Northwest, Gary, IN 46408

Corresponding Author: rdziar{at}iun.edu

Skin and mucous membranes come in contact with external environment and protect tissues from infections by producing antimicrobial peptides. We report that human Peptidoglycan Recognition Proteins 3 and 4 (PGLYRP3 and PGLYRP4) are secreted as 89-115 kDa disulfide-linked homo- and heterodimers and are bactericidal against several pathogenic and nonpathogenic transient, but not normal flora, Gram-positive bacteria. PGLYRP3 and PGLYRP4 are also bacteriostatic towards all other tested bacteria, which include Gram-negative bacteria and normal flora Gram-positive bacteria. PGLYRP3 and PGLYRP4 are also active in vivo and protect mice against experimental lung infection. In contrast to antimicrobial peptides, PGLYRPs kill bacteria by interacting with their cell wall peptidoglycan, rather than permeabilizing their membranes. PGLYRP3 and PGLYRP4 are expressed in the skin, eyes, salivary glands, throat, tongue, esophagus, stomach, and intestine. Thus, we have identified the function of mammalian PGLYRP3 and PGLYRP4, and show that they are a new class of bactericidal and bacteriostatic proteins that have different structure, mechanism of action, and expression pattern than antimicrobial peptides.

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