|Protein Name||Peptidoglycan recognition protein 1|
|Ref Sequence Id||NP_776998.1|
|Amino Acid Lenth||190|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||neutrophils, eosinophil, bone marrow, fetal liver|
|Protein Function||pattern recognition molecules of innate immunity; bind bacterial molecules and kill in peptidoglycan independent manner; recognizes multiple microbial components|
|Biochemical Properties||highest affinity for lipopolysaccharide; significant affinity for lipotechoic acid and little for peptidoglycan in killing inhibition assays; MgCl2 or CaCl2 as low as 0.8 mM ablate bPGRP-S-mediated killing of S. typhimurium; bPGRP-S has a serine substitution at a cysteine residue predicted to stabilize a zinc ion; PGRP in camel ripe and porcine colostral milk is a 19-kDa monomeric protein;|
|Significance in milk||As found in camel milk it exhibits udder protection; control lactic acid bacteria; upregulated in cases of mastitis; avidly bound to lactic acid bacteria, and the protein was markedly upregulated in the case of streptococcal infection;|
|Additional Comments||In mammals, PRPs are differentially expressed in the bone marrow, liver, and esophagus where they are likely to play a role in recognition of bacteria|
|Bibliography||1. Kappeler, S. R., Heuberger, C., Farah, Z., & Puhan, Z. (2004). Expression of the peptidoglycan recognition protein, PGRP, in the lactating mammary gland. Journal of Dairy Science, 87(8), 2660–2668. https://doi.org/10.3168/jds.S0022-0302(04)73392-5. |
2. Dziarski, R. (2004). Peptidoglycan recognition proteins (PGRPs). Molecular Immunology, 40(12), 877–886. https://doi.org/10.1016/j.molimm.2003.10.011.
3. Tydell, C. C., Yuan, J., Tran, P., & Selsted, M. E. (2006). Bovine peptidoglycan recognition protein-S: antimicrobial activity, localization, secretion, and binding properties. Journal of Immunology (Baltimore, Md. : 1950), 176(2), 1154–1162. https://doi.org/10.4049/jimmunol.176.2.1154.