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PR-39, a multifunctional antibacteri...
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Shi, Jishu.
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PR-39, a multifunctional antibacterial peptide.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
PR-39, a multifunctional antibacterial peptide./
作者:
Shi, Jishu.
面頁冊數:
148 p.
附註:
Source: Dissertation Abstracts International, Volume: 57-01, Section: B, page: 0231.
Contained By:
Dissertation Abstracts International57-01B.
標題:
Health Sciences, Immunology. -
電子資源:
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.
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Source: Dissertation Abstracts International, Volume: 57-01, Section: B, page: 0231.
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Thesis (Ph.D.)--Kansas State University, 1995.
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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.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9614290
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