ChBac3.4: A Novel Proline-Rich Antimicrobial Peptide from Goat Leukocytes

Shamova, O. V.; Орлов, Д. С.; Stegemann, Christin; Czihal, Patricia; Hoffmann, Ralf; Brogden, Kim A.; Колодкин, Н. И.; Сакута, Г А; Tossi, Alessandro; Sahl, Hans‐Georg; Kokryakov, V. N.; Lehrer, Robert I.

doi:10.1007/s10989-008-9159-7

Cited by 40 publications

(45 citation statements)

References 49 publications

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“…The first to be identified, Bac5 and Bac7, were isolated in our laboratory from bovine neutrophils (see Table 1) [10,22], later followed by a putative pseudogene containing the sequence of a third bovine PR-AMP, Bac4 [23]. Their orthologues have been identified in other bovids, including sheep and goat [24], while additional members have been detected or purified in sheep, including OABac11 and OABac6 [25]. Pig leukocytes express other PR-AMPs, PR-39 [26] and prophenins [27].…”

Section: Diversity Of Proline-rich Antimicrobial Peptidesmentioning

confidence: 99%

“…Among the Gram-positive species, only those that are in any case known to be easily killed by AMPs in general, such as Bacillus megaterium, Bacillus subtilis and Listeria monocytogenes, are affected, albeit at higher concentrations [10,24,26,50,51]. PR-39 was found to be active against drug-susceptible and multi-drug-resistant clinical isolates of Mycobacterium tuberculosis [52], while Bac5 and Bac7 were reported to be active against various species of Brucella [53] as well as against spirochetes, such as Leptospira but not Borrelia species [54].…”

Section: Antimicrobial and Other Host Defence Activities Of Prampsmentioning

confidence: 99%

“…Shortening from the N-terminus, the most cationic region in all three peptides, is instead deleterious, and fragments comprising the central or C-terminal regions such as Bac7(29-56), Bac5 and PR-39 (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26) are poorly active or inactive, despite having a considerable residual cationicity [9,55]. This trend has also been observed in naturally occurring N-and C-terminal fragments of the sheep bactenecins OaBac5 or OaBac7.5 [56].…”

Section: Conformation and Structure-activity Relationshipsmentioning

confidence: 99%

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Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action

Scocchi

Tossi

Gennaro

2011

Cell. Mol. Life Sci.

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204

257

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Proline-rich antimicrobial peptides are a group of cationic host defense peptides of vertebrates and invertebrates characterized by a high content of proline residues, often associated with arginine residues in repeated motifs. Those isolated from some mammalian and insect species, although not evolutionarily related, use a similar mechanism to selectively kill Gram-negative bacteria, with a low toxicity to animals. Unlike other types of antimicrobial peptides, their mode of action does not involve the lysis of bacterial membranes but entails penetration into susceptible cells, where they then act intracellularly. Some aspects of the transport system and cytoplasmic targets have been elucidated. These features make them attractive both as anti-infective lead compounds and as a new class of potential cell-penetrating peptides capable of internalising membrane-impermeant drugs into both bacterial and eukaryotic cells.

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Section: Diversity Of Proline-rich Antimicrobial Peptidesmentioning

confidence: 99%

Section: Antimicrobial and Other Host Defence Activities Of Prampsmentioning

confidence: 99%

Section: Conformation and Structure-activity Relationshipsmentioning

confidence: 99%

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Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action

Scocchi

Tossi

Gennaro

2011

Cell. Mol. Life Sci.

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204

257

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“…The ovine peptide SMAP29 (RGLRRLGRKIAHGV KKYGPTVLRIIRIA-NH 2 ) has been synthesized and has broad-spectrum activity through permeabilization of the outer and inner membrane of the bacterial cell (Skerlavaj et al 1999). OaBac5mini peptide (RFRPPI RRPPIPPFRPPFRPPVR-NH 2 ) was based on OaBac5 which is a 51-residue proline-and arginine-rich peptide that has been isolated from ovine neutrophils (Anderson and Yu 2003;Shamova et al 1999). OaBac5mini is synthesized as a truncated version of OaBac5 and comprises 6 N-terminal residues, one copy of the 16-residue repeat and the first 2 residues of the second repeat (Anderson et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Synergistic effects of ovine-derived cathelicidins and other antimicrobials against Escherichia coli O157:H7 and Staphylococcus aureus 1056 MRSA

et al. 2009

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Synergistic effects of ovine-derived cathelicidins SMAP29 and OaBac5mini with the antimicrobials polymyxin B, lysozyme, nisin and lactoferrin were investigated against E. coli O157:H7 and S. aureus 1056 MRSA. Lysozyme showed synergy against E. coli O157:H7 with SMAP29, polymyxin B and lactoferrin. Synergy was also found between SMAP29 and lactoferrin against this host. Against S. aureus 1056 MRSA, lysozyme showed synergy with OaBac5mini, polymyxin B and nisin, while synergy was also found between nisin and OaBac5mini and polymyxin B. Other combinations of the antimicrobials were either additive or non-synergistic.

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“…Prior to our work, only two variants of the predicted peptide OaBac5 had been isolated from ovine neutrophils (Shamova et al 1999). In addition to these, we isolated the originally predicted OaBac5 and another OaBac5 variant, the C-terminus of the predicted OaBac7.5, and various truncated forms of OaBac11.…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial fragments of the pro-region of cathelicidins and other immune peptides

Anderson

Rehders

2008

Biotechnol Lett

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In addition to the numerous cathelicidin peptides that are associated with the antimicrobial activity exhibited by a crude extract from ovine blood, a further three peptides with antimicrobial activity have been identified. These were part of the precursor cathelin domain of cathelicidins, a large fragment of platelet factor 4 and a small peptide similar to signal peptide of the T-cell glycoprotein CD4 precursor. Fragments of proteins that are involved in protecting the host from infection may have a secondary purpose as antimicrobial agents once they have carried out their primary purpose and are cleaved the main protein.

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ChBac3.4: A Novel Proline-Rich Antimicrobial Peptide from Goat Leukocytes

Cited by 40 publications

References 49 publications

Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action

Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action

Synergistic effects of ovine-derived cathelicidins and other antimicrobials against Escherichia coli O157:H7 and Staphylococcus aureus 1056 MRSA

Antimicrobial fragments of the pro-region of cathelicidins and other immune peptides

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