cDNA sequences of three sheep myeloid cathelicidins

Bagella, Luigi; Scocchi, Marco; Zanetti, Margherita

doi:10.1016/0014-5793(95)01285-3

Cited by 102 publications

(82 citation statements)

References 40 publications

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“…This molecule is a new member of a large family of antimicrobial peptide precursors found in human (13,28), pig (6,8,14,29,30), cow (9, 31), rabbit (12), and sheep (10,11). The homology among the precursors of these antimicrobial peptides lies in a common NH 2 -terminal region of the unprocessed precursor known as cathelin and has led to use of the term cathelicidins to describe the gene family.…”

Section: Discussionmentioning

confidence: 99%

Identification of CRAMP, a Cathelin-related Antimicrobial Peptide Expressed in the Embryonic and Adult Mouse

Gallo

Kim

Bernfield

et al. 1997

Journal of Biological Chemistry

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372

319

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Cathelicidins are the precursors of potent antimicrobial peptides that have been identified in several mammalian species. Prior work has suggested that members of this gene family can participate in host defense through their antimicrobial effects and activate mesenchymal cells during wound repair. To permit further study of these proteins a reverse transcriptase-polymerase chain reaction approach was used to identify potential mouse homologs. A full-length 562-base pair cDNA clone was obtained encoding an NH 2 -terminal prepro domain homologous to other cathelicidins and a unique COOH-terminal peptide. This gene, named Cramp for cathelin-related antimicrobial peptide, was mapped to chromosome 9 at a region of conserved synteny to which genes for cathelicidins have been mapped in pig and man. Northern blot analysis detected a 1-kilobase transcript that was expressed in adult bone marrow and during embryogenesis as early as E12, the earliest stage of blood development. Reverse transcriptase-polymerase chain reaction also detected CRAMP expression in adult testis, spleen, stomach, and intestine but not in brain, liver, heart, or skeletal muscle. To evaluate further the expression and function of CRAMP, a peptide corresponding to the predicted COOH-terminal region was synthesized. CD spectral analysis showed that CRAMP will form an amphipathic ␣-helix similar to other antimicrobial peptides. Functional studies showed CRAMP to be a potent antibiotic against Gram-negative bacteria by inhibiting growth of a variety of bacterial strains (minimum inhibitory concentrations 0.5-8.0 M) and by permeabilizing the inner membrane of Escherichia coli directly at 1 M. Antiserum against CRAMP revealed abundant expression in myeloid precursors and neutrophils. Thus, CRAMP represents the first antibiotic peptide found in cells of myeloid lineage in the mouse. These data suggest that inflammatory cells in the mouse can use a nonoxidative mechanism for microbial killing and permit use of the mouse to study the role such peptides play in host defense and wound repair.

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Section: Discussionmentioning

confidence: 99%

Identification of CRAMP, a Cathelin-related Antimicrobial Peptide Expressed in the Embryonic and Adult Mouse

Gallo

Kim

Bernfield

et al. 1997

Journal of Biological Chemistry

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372

319

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“…Thus, the novel peptide of this work is proposed to be a new pleurocidin-like peptide. According to posttranslational modification principles, a putative proteolytic cleavage site existed, we suggested that the mature peptide containing 24 amino-acid residues with the glycine following arginine was processed to a C-terminal amide, [19][20][21] and designated HKPLP (Hi. K. Bleeker pleurocidin-like peptide).…”

Section: Sequence Analysismentioning

confidence: 99%

Identification, synthesis and characterization of a novel antimicrobial peptide HKPLP derived from Hippocampus kuda Bleeker

Sun

Jing

et al. 2012

J Antibiot

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A novel gene encoding 55 amino-acid residues has been identified from the brooding pouch cDNA library of Hippocampus kuda Bleeker. The deduced amino-acid sequence is highly homologous to several pleurocidin-like peptides from the winter flounder and comprises a signal peptide, a pro-peptide and a mature peptide. The glycine-rich mature peptide, designated HKPLP, contains 24 amino-acid residues and has been synthesized by solid-phase peptide synthesis. The purified HKPLP exhibits antimicrobial activity against several Gram-positive and Gram-negative bacterial strains at low concentrations (MIC 1.5-7.5 lM). Thermal stability assay data show good heat stability. CD spectroscopy experiments indicate that the dominant contents are anti-parallel and parallel sheets, which may have b-sheet or b-strand motif. It is inferred that HKPLP participates in the host defense during egg fertilization and embryo development as an antimicrobial peptide in brooding pouch.

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“…The structure and composition of SMAP29 (also known as SC5) was first deduced from sheep myeloid DNA [44,45] and later synthesized to assess its antimicrobial activity [11,43,46]. SMAP29 has broad-spectrum antimicrobial activity against Gramnegative and Gram-positive bacteria and fungi [11,43,45,46], is active in both low and high ionic strength conditions [11], and induces significant morphological alterations in bacterial surfaces [46,48].…”

Section: Cationic Antimicrobial Peptidesmentioning

confidence: 99%

Antimicrobial peptides in animals and their role in host defences

Brogden

Ackermann

McCray

et al. 2003

International Journal of Antimicrobial Agents

418

287

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Domesticated animals have a large variety of antimicrobial peptides that serve as natural innate barriers limiting microbial infection or, in some instances, act as an integral component in response to inflammation or microbial infection. These peptides differ in size, composition, mechanisms of activity and range of antimicrobial specificities. They are expressed in many tissues, polymorphonuclear leukocytes, macrophages and mucosal epithelial cells. There is a small group of anionic antimicrobial peptides found in ruminants and a much larger group of cationic antimicrobial peptides found in all domesticated animals. The cationic peptides include linear, helical peptides, linear peptides rich in proline and cysteine-stabilized peptides with a b-sheet and are commonly referred to as cathelicidins and defensins. These peptides are generally broad-spectrum for Gram-positive bacteria, Gram-negative bacteria and fungi (e.g. myeloid antimicrobial peptides, a-, bdefensins, and protegrins) or are specific to one of these groups (e.g. porcine cecropin P1, Bac5, Bac7, PR-39 and prophenin). RightsWorks produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted. Abstract Domesticated animals have a large variety of antimicrobial peptides that serve as natural innate barriers limiting microbial infection or, in some instances, act as an integral component in response to inflammation or microbial infection. These peptides differ in size, composition, mechanisms of activity and range of antimicrobial specificities. They are expressed in many tissues, polymorphonuclear leukocytes, macrophages and mucosal epithelial cells. There is a small group of anionic antimicrobial peptides found in ruminants and a much larger group of cationic antimicrobial peptides found in all domesticated animals. The cationic peptides include linear, helical peptides, linear peptides rich in proline and cysteine-stabilized peptides with a b-sheet and are commonly referred to as cathelicidins and defensins. These peptides are generally broad-spectrum for Gram-positive bacteria, Gram-negative bacteria and fungi (e.g. myeloid antimicrobial peptides, a-, b-defensins, and protegrins) or are specific to one of these groups (e.g. porcine cecropin P1, Bac5, Bac7, PR-39 and prophenin). Published by Elsevier B.V.

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cDNA sequences of three sheep myeloid cathelicidins

Cited by 102 publications

References 40 publications

Identification of CRAMP, a Cathelin-related Antimicrobial Peptide Expressed in the Embryonic and Adult Mouse

Identification of CRAMP, a Cathelin-related Antimicrobial Peptide Expressed in the Embryonic and Adult Mouse

Identification, synthesis and characterization of a novel antimicrobial peptide HKPLP derived from Hippocampus kuda Bleeker

Antimicrobial peptides in animals and their role in host defences

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