Antibacterial peptides from pig intestine: isolation of a mammalian cecropin.

Lee, Jong-Youn; Boman, Anita; Sun, Chuanxin; Andersson, Mats; Jörnvall, Hans; Mutt, Viktor; Boman, Hans G.

doi:10.1073/pnas.86.23.9159

Cited by 394 publications

(276 citation statements)

References 17 publications

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“…This peptide and the homologous peptide derived from rabbit CAP18 (Tossi, A. et al, unpublished) are new examples of a-helical antibacterial peptides. This structural motif is common in insect 1251 and amphibian [26} antibacterial peptides, but to our knowledge was not found in mammalian antibacterial peptides, with the possible exception of porcine Pl cecropin [28]. Furthermore, PMAP-36 and the C-terminal domain of CAP18 are the only antibacterial peptides derived from cathelin-containing precursors with an amphipathic a-helical motif.…”

Section: Pimentioning

confidence: 84%

Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA

et al. 1994

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Several myeloid precursors of antibacterial peptides have recently been shown to share homologous pre-and pro-regions. Taking advantage of this homology, a novel cDNA was cloned from pig bone marrow RNA. This encodes a 166-residue polypeptide with highly conserved pre-(29 residues) and pro-(101 residues) sequences, followed by a unique, 36-residue C-terminal sequence. Structure analyses of this C-terminal region have identified a highly cationic sequence predicted to adopt an amphipathic a-helical conformation. A peptide corresponding to this sequence was chemically synthesized and shown to arrest the growth of both Gram-positive and Gram-negative bacteria. At least for Escherichia coli, the activity of this peptide appears to be mediated by its ability to permeabilize the bacterial membranes.

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Section: Pimentioning

confidence: 84%

Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA

et al. 1994

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“…A cecropin homologue has been described in extracts of the pig intestine (15), but studies aimed at cloning the corresponding gene in pigs have remained so far inconclusive. Cecropins were shown to permeabilize the bacterial membranes through their amphipathic helix structure (12).…”

Section: (1) Cecropinsmentioning

confidence: 99%

Antimicrobial peptide defense in Drosophila

1997

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Drosophila responds to a septic injury by the rapid synthesis of antimicrobial peptides. These molecules are predominantly produced by the fat body, a functional equivalent of mammalian liver, and are secreted into the hemolymph where their concentrations can reach up to 100 μM. Six distinct antibacterial peptides (plus isoforms) and one antifungal peptide have been characterized in Drosophila and their genes cloned. The induction of the gene encoding the antifungal peptide relies on the spätzle/Toll/cactus gene cassette, which is involved in the control of dorsoventral patterning in the embryo, and shows interesting structural and functional similarities with cytokine‐induced activation of NF‐ϰB in mammalian cells. An additional pathway, dependent on the as yet unidentified imd (for immune‐deficiency) gene, is required for the full induction of the antibacterial peptide genes. Mutants deficient for the Toll and imd pathways exhibit a severely reduced survival to fungal and bacterial infections, respectively. Recent data on the molecular mechanisms underlying recognition of non‐self are also discussed in this review.

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“…In 1989, the first mammalian cecropin was isolated from pig small intestine [12]. This peptide, porcine cecropin P1, presents extensive homology with insect cecropins except that it is not amidated on the C-terminus.…”

Section: Structural Properties Of Secretolytinmentioning

confidence: 99%

“…Later, an antibacterial peptide with 33% homology to insect cecropins was isolated from porcine small intestine [12]. More recently, a new antibacterial peptide was isolated from pig myeloid cells (PMAP-37): its sequence also shows a high degree of similarity with the N-terminal helix of cecropin domain [13].…”

Section: Introductionmentioning

confidence: 99%

Antibacterial activity of secretolytin, a chromogranin B‐derived peptide (614–626), is correlated with peptide structure

et al. 1996

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Amongst the chromogranin B (CGB) derived fragments naturally generated in bovine chromaffin granules and detected in the extracellular space, we recently identified a major peptide corresponding to the 614--626 sequence of CGB. This peptide, named secretolytin, shared an interesting sequence homology with the lyric domain of cecropins and displayed a potent antibacterial activity. The aim of the present study was to determine the structural features of secretolytin necessary for this biological activity. Our results suggest that an a-helical amphipathic structure common to secretolytin, cecropins and pig myeloid antibacterial peptide may account for the antibacterial activity.

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Antibacterial peptides from pig intestine: isolation of a mammalian cecropin.

Cited by 394 publications

References 17 publications

Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA

Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA

Antimicrobial peptide defense in Drosophila

Antibacterial activity of secretolytin, a chromogranin B‐derived peptide (614–626), is correlated with peptide structure

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