Molecular cloning of a putative homolog of proline/arginine‐rich antibacterial peptides from porcine bone marrow

Pungerčar, Jože; Štrukelj, Borut; Kopitar, Gregor; Renko, M.; Lenarčič, Brigita; Gubenšek, Franc; Türk, Vito

doi:10.1016/0014-5793(93)80821-b

Cited by 43 publications

(40 citation statements)

References 25 publications

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“…Pungercar et al [30] recently obtained from porcine bone marrow and sequenced two cDNA clones, C12 and C6, that encoded virtually identical proline and arginine rich antimicrobial peptides at the C-terminus of a cathelin-containing prepropeptide. The translated sequence of clone C 12 included a 30 residue, N-terminal signal peptide followed by a 198 residue protein whose N-terminal region was 84% identical to porcine cathelin in primary sequence.…”

Section: Discussionmentioning

confidence: 99%

Prophenin‐1, an exceptionally proline‐rich antimicrobial peptide from porcine leukocytes

Harwig

Kokryakov²,

Swiderek

et al. 1995

FEBS Letters

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We purified and characterized an unusual antimicrobial peptide, prophenin-1 (PF-I), from porcine leukocytes. The peptide had a mass of 8,683 and contained 79 residues, including 42 (53.2%) prolines and 15 (19.0%) phenylalanines. Its N-terminal 60 residues consisted of three perfect and three nearly perfect repeats of a decamer, FPPPNFPGPR. Prophenin-I was encoded on a cathelin-containing precursor and showed substantially more activity against E. coli, a Gram-negative bacterium, than against Listeria monocytogenes, a Gram-positive organism, in vitro.

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Section: Discussionmentioning

confidence: 99%

Prophenin‐1, an exceptionally proline‐rich antimicrobial peptide from porcine leukocytes

Harwig

Kokryakov²,

Swiderek

et al. 1995

FEBS Letters

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“…If the prosequence were cleaved after the valine, which is the common cleavage site, as in the case of cathelin and several other cathelicidins [90], prophenin precursors would be processed into a 97-residue mature peptide. However, the actual mature products are prophenins-1 and -2, which contain only the C-terminal 79 residues.…”

Section: Prophenins Prolinephenylalanine-rich Amps With Repeated Decmentioning

confidence: 99%

Porcine antimicrobial peptides: New prospects for ancient molecules of host defense

Zhang¹,

Ross²,

Blecha³

2000

Vet. Res.

110

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-Antimicrobial peptides (AMPs) are small, endogenous, polycationic molecules that constitute a ubiquitous and significant component of innate immunity. These natural antibiotics have broad microbicidal activity against various bacteria, fungi, and enveloped viruses. Because most AMPs kill bacteria by physical disruption of cell membranes, which may prevent microorganisms from developing resistance against these agents, they are being explored as possible alternatives to conventional antibiotics. Pigs, like many other mammals, produce an impressive array of AMPs, which are synthesized predominantly by host leukocytic phagocytes or mucosal epithelial cells. Currently, more than a dozen distinct porcine AMPs have been identified and a majority belongs to the cathelicidin family. This review briefly summarizes recent advances in porcine AMP research with an emphasis on the diverse biological functions of each peptide. Mechanisms of action of these AMPs and their role in the resistance to infections are considered. Finally, the current status of pharmaceutical and agricultural uses of AMPs as well as future prospects for their application in the food animal industry is discussed.pig / antimicrobial peptide / cathelicidin / defensin / innate immunity Résumé -Peptides antimicrobiens porcins : nouvelles perspectives pour d'anciennes molécules de défense de l'hôte. Les peptides antimicrobiens sont de petites molécules endogènes, polycationiques, qui représentent un élément important et ubiquitaire des défenses immunes naturelles. Ces antibiotiques naturels ont un effet antimicrobien à large spectre, à la fois contre des bactéries, des moisissures et des virus enveloppés. Comme la plupart de ces peptides antimicrobiens tuent les bactéries par altération physique de leur membrane, ce qui peut éviter le développement de souches microbiennes résistantes à ces agents, ils représentent des alternatives possibles à l'emploi des antibiotiques classiques. Le porc, comme de nombreux autres mammifères, produit une gamme importante de peptides antimicrobiens, synthétisés pour l'essentiel par les leucocytes à activité phagocytaire, ou par les cellules épithéliales des muqueuses. Il y a actuellement plus d'une douzaine de peptides antimicrobiens identifiés chez le porc, dont la majorité fait partie de la famille des cathélicidines. Cet article résume les progrès récents accomplis dans le domaine des peptides antimicrobiens du porc, Vet. Res. 31 (2000) 277-296 277

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“…In some cases, both peptide isolation and cDNA cloning have been accomplished. For example, Pungercar et al obtained two cDNA clones from porcine bone marrow, 'clone-12' and 'clone-6', that encoded nearly identical proline-rich antimicrobial peptides [18,19] and we independently purified the corresponding mature peptides, Prophenin (PF)-I and 2, from porcine leukocytes [17]. *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

“…Recent cDNA cloning studies have revealed that many structurally and functionally diverse leukocyte antimicrobial peptides share a highly conserved pro-region, known as the 'cathelin' domain. Among these are bovine indolicidin, cyclic dodecapeptide, Bac 5 and Bac 7 [2 7]; rabbit 'P15' and CAP 18 [8][9][10][11]; porcine PR-39 [12,13], protegrins [14][15][16], prophenins [17][18][19], PMAP-23, PMAP-36 and PMAP-37 [20][21][22]; and human FALL-39/CAP-18 [23,24].…”

Section: Introductionmentioning

confidence: 99%

Structures of genes for two cathelin‐associated antimicrobial peptides: prophenin‐2 and PR‐39

1995

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We characterized genes for prophenin (PF)-2 and PR-39, two cathelin-associated antimicrobial peptides found in porcine leukocytes. Both contained 4 exons and 3 introns and were compact, contiguous and highly homologous. Exons I-III encoded most of their cathelin domains. Exon IV specified the final few cathelin residues, including its conserved C-terminal valine, followed by the mature PR-39 peptide or a PF-2 precursor. The highly conserved 5' flanking sequences of this gene family contained NF-~cB, IL-6, GM-CSF and NF-! binding motifs and the introns were unusually conserved. These data suggest that the panoply of porcine cathelin-associated antimicrobial peptides arose relatively recently via gene reduplications and exon shuffling, and that in vivo expression of cathelin-associated antimicrobial peptides may respond to mediators generated early during infection.

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Molecular cloning of a putative homolog of proline/arginine‐rich antibacterial peptides from porcine bone marrow

Cited by 43 publications

References 25 publications

Prophenin‐1, an exceptionally proline‐rich antimicrobial peptide from porcine leukocytes

Prophenin‐1, an exceptionally proline‐rich antimicrobial peptide from porcine leukocytes

Porcine antimicrobial peptides: New prospects for ancient molecules of host defense

Structures of genes for two cathelin‐associated antimicrobial peptides: prophenin‐2 and PR‐39

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