Congeners of SMAP29 Kill Ovine Pathogens and Induce Ultrastructural Damage in Bacterial Cells

Kalfa, V. C.; Jia, Hong Peng; Kunkle, Robert A.; McCray, Paul B.; Tack, Brian F.; Brogden, Kim A.

doi:10.1128/aac.45.11.3256-3261.2001

Cited by 82 publications

(84 citation statements)

References 15 publications

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“…In a recent study, the size and the amino acid composition of SMAP29 was systematically altered to create a family of 23 related peptides [48]. SMAP28, SMAP29, and a derivative of SMAP29 called ovispirin were all effective against Gram-negative bacteria (MIC range 0.1 Á/10.0 mg/l), Gram-positive bacteria (MIC range 0.8 to !/20.0 mg/l), and Aspergillus fumigatus (MIC 2.5 mg/l).…”

Section: Cationic Antimicrobial Peptidesmentioning

confidence: 99%

“…SMAP28-NH 2 is thought to be the native form of the peptide [45,46] and synthesized SMAP28-NH 2 is antimicrobial [48]. Only recently, SMAP28-NH 2 has been isolated directly from ovine neutrophils (M. Ferguson, K. Brogden and B.…”

Section: Cationic Antimicrobial Peptidesmentioning

confidence: 99%

“…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]. Its activity against multiple antibiotic-resistant pathogens from patients with cystic fibrosis is of particular interest [47].…”

Section: Cationic Antimicrobial Peptidesmentioning

confidence: 99%

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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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Section: Cationic Antimicrobial Peptidesmentioning

confidence: 99%

Section: Cationic Antimicrobial Peptidesmentioning

confidence: 99%

Section: Cationic Antimicrobial Peptidesmentioning

confidence: 99%

See 1 more Smart Citation

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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“…Ovispirin-1 (OVIS) is an 18-amino acid (KNLRR IIRKI IHIIK KYG) helical peptide, and has significant antimicrobial activity [22]. It is unsuitable for therapeutic use owing to its hemolytic properties [22]. Novispirin-G10 (KNLRR IIRKG IHIIK KYG) and novispirin-T7 (KNLRR ITRKI IHIIK KYG) are single residue mutants of OVIS which retain the antibacterial activity, but are less toxic.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Molecular dynamics investigation of the influence of anionic and zwitterionic interfaces on antimicrobial peptides’ structure: Implications for peptide toxicity and activity

Khandelia

Kaznessis

2006

Peptides

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Molecular dynamics simulations of three related helical antimicrobial peptides have been carried out in zwitterionic diphosphocholine (DPC) micelles and anionic sodiumdodecylsulfate (SDS) micelles. These systems can be considered as model mammalian and bacterial membrane interfaces, respectively. The goal of this study is to dissect the differences in peptide composition which make the mutant peptides (novispirin-G10 and novispirin-T7) less toxic than the parent peptide ovispirin (OVIS), although all three peptides have highly antibacterial properties. Compared to G10 and T7, OVIS inserts deepest into the DPC micelle. This correlates well with the lesser toxicity of G10 and T7. There is strong evidence which suggests that synergistic binding of hydrophobic residues drives binding of OVIS to the micelle. The helical content of G10 and T7 is reduced in the presence of DPC, and this leads to less amphipathic peptide structures, which bind weakly to the micelle. Simulations in SDS were carried out to compare the influence of membrane electrostatics on peptide structure. All three peptides bound strongly to SDS, and retained helical form. This corresponds well with their equally potent antibacterial properties. Based on the simulations, we argue that secondary structure stability often leads to toxic properties. We also propose that G10 and T7 operate by the carpet mechanism of cell lysis. Toxicity of peptides operating by the carpet mechanism can be attenuated by reducing the peptide helical content. The simulations successfully capture experimental binding states, and the different depths of binding of the three peptides to the two micelles correlate with their antibacterial and toxic properties.

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Development of Antimicrobial Peptides as Therapeutic Agents

Hodges

Jiang

Whitehurst

et al. 2011

Pharmaceutical Sciences Encyclopedia

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Classical antibiotics work by inhibiting bacterial cell wall synthesis, protein synthesis, DNA (deoxyribonucleic acid) replication, or by modifying metabolism. Bacteria can resist antibiotics as a result of chromosomal changes (mutation or inductive expression of a latent chromosomal gene) or the exchange of genetic material via plasmids and transposons. As this chapter will discuss, antibiotics are rendered inactive by three major mechanisms: (1) antibiotic inactivation by destruction or modification, (2) prevention of access of the antibiotic to the target, and (3) alteration of the target site of the antibiotic. Bacteria have a remarkable ability to overcome each new reagent synthesized as a potential classical antibiotic. Consequently, the current priority is the development of alternative drugs and/or the isolation of native molecules that would allow the consistent and proper control of pathogen‐caused diseases.

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Congeners of SMAP29 Kill Ovine Pathogens and Induce Ultrastructural Damage in Bacterial Cells

Cited by 82 publications

References 15 publications

Antimicrobial peptides in animals and their role in host defences

Antimicrobial peptides in animals and their role in host defences

Molecular dynamics investigation of the influence of anionic and zwitterionic interfaces on antimicrobial peptides’ structure: Implications for peptide toxicity and activity

Development of Antimicrobial Peptides as Therapeutic Agents

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