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PR-39, a multifunctional antibacteri...

Shi, Jishu.

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PR-39, a multifunctional antibacterial peptide.

Record Type:	Electronic resources : Monograph/item
Title/Author:	PR-39, a multifunctional antibacterial peptide./
Author:	Shi, Jishu.
Description:	148 p.
Notes:	Source: Dissertation Abstracts International, Volume: 57-01, Section: B, page: 0231.
Contained By:	Dissertation Abstracts International57-01B.
Subject:	Health Sciences, Immunology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9614290

PR-39, a multifunctional antibacterial peptide.
Shi, Jishu.

PR-39, a multifunctional antibacterial peptide. - 148 p.

Source: Dissertation Abstracts International, Volume: 57-01, Section: B, page: 0231.

Thesis (Ph.D.)--Kansas State University, 1995.

A proline-arginine-rich antibacterial peptide (PR-39) from pig neutrophils was isolated and characterized by gel-filtration, reversed-phase high performance liquid chromatography (RP-HPLC), mass spectrometry, and various antibacterial assays. PR-39 was a potent antibiotic mainly against Gram-negative bacteria such as Escherichia coli and salmonellae. PR-39 had postantibiotic effect and inhibited Salmonella typhimurium invasion into rat intestinal epithelial cells. This antibacterial peptide killed bacteria by a nonmembrane pore-forming mechanism.Subjects--Topical Terms:

1017716
Health Sciences, Immunology.

PR-39, a multifunctional antibacterial peptide.
LDR:02675nmm 2200253 4500 001 1841278
005 20050908073011.5
008 130614s1995 eng d
035 $a (UnM)AAI9614290
035 $a AAI9614290
040 $a UnM $c UnM
100 1 $a Shi, Jishu. $3 1929584
245 1 0 $a PR-39, a multifunctional antibacterial peptide.
300 $a 148 p.
500 $a Source: Dissertation Abstracts International, Volume: 57-01, Section: B, page: 0231.
502 $a Thesis (Ph.D.)--Kansas State University, 1995.
520 $a A proline-arginine-rich antibacterial peptide (PR-39) from pig neutrophils was isolated and characterized by gel-filtration, reversed-phase high performance liquid chromatography (RP-HPLC), mass spectrometry, and various antibacterial assays. PR-39 was a potent antibiotic mainly against Gram-negative bacteria such as Escherichia coli and salmonellae. PR-39 had postantibiotic effect and inhibited Salmonella typhimurium invasion into rat intestinal epithelial cells. This antibacterial peptide killed bacteria by a nonmembrane pore-forming mechanism.
520 $a In a structure-activity relationship study, it was determined that the first 26 amino acids of the NH $\ sb2 $- terminus (PR-26) was the antibacterial functional domain of PR-39. The N-terminal first three arginine residues and the central segment containing residues 20 to 26 were essential for the antibacterial activity of PR-26. In addition, PR-39 inhibited the production of superoxide anion (O $\ sb2\sp- $) from pig neutrophils in a whole cell assay and human neutrophils in a cell-free assay. Using a cell-free superoxide anion assay and recombinant phagocyte NADPH oxidase components, we demonstrated that PR-39 bound to the Src homology region 3 (SH3) domains of p47 $\ sp{phox}, $ one of the cytosol components of phagocyte NADPH oxidase, and blocked the interaction of p47 $\ sp{phox} $ with p22 $\ sp{phox}, $ one of the transmembrane protein components of phagocyte NADPH oxidase. This suggested that PR-39 might be a negative regulator for phagocyte NADPH oxidase and have antioxidant activity in host inflammatory responses.
520 $a Taken together, these findings show that a multifunctional antibacterial peptide, PR-39, is found in pig neutrophils. The study of PR-39 will generate new information about how the neutrophil regulates its antimicrobial systems in host defense and will provide an excellent candidate for the development of new drugs for infectious diseases.
590 $a School code: 0100.
650 4 $a Health Sciences, Immunology. $3 1017716
690 $a 0982
710 2 0 $a Kansas State University. $3 1017593
773 0 $t Dissertation Abstracts International $g 57-01B.
790 $a 0100
791 $a Ph.D.
792 $a 1995
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9614290