Casocidin‐I: a casein‐α<sub>s2</sub> derived peptide exhibits antibacterial activity

Zucht, Hans-Dieter; Raida, Manfred; Adermann, Knut; Mägert, Hans-Jürgen; Forssmann, Wolf‐Georg

doi:10.1016/0014-5793(95)00974-e

Cited by 184 publications

(133 citation statements)

References 30 publications

Supporting

Mentioning

123

Contrasting

Unclassified

Order By: Relevance

“…Previous bioassays showed that the synthetic peptide casocidin-I exhibits an antibacterial effect (Zucht et al, 1995), and antimicrobial milk proteins, such as lactoferrin and its pepsin-derived peptide fragments (lactoferricins) and isracidin, were also described previously (Yamauchi et al, 1993;Lahov and Regelson, 1996). Casocidin-I was identified by LC-MS/MS in a series of protein spots with an Mr of 48.7 kDa and a pI of approximately 10.08 (Table 1).…”

Section: Discussionmentioning

confidence: 54%

Comparative proteomic changes of differentially expressed whey proteins in clinical mastitis and healthy yak cows

Li¹,

Ding²,

Wan³

et al. 2014

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT. Under the traditional grazing system on the QinghaiTibetan Plateau, the amount of milk in domesticated yak (Bos grunniens) with clinical mastitis decreases and the milk composition is altered. To understand the mechanisms of mammary gland secreted milk and disease infection, changes in the protein composition of milk during clinical mastitis were investigated using a proteomic approach. Milk whey from yak with clinical mastitis was compared to whey from healthy animals with two-dimensional gel electrophoresis using a mass spectrometer. Thirteen protein spots were identified to be four differentially expressed proteins. Increases in the concentrations of proteins of blood serum origin, including lactoferrin, were identified in mastitic whey compared to normal whey, while concentrations of the major whey proteins, casocidin-I, a-lactalbumin, and b-lactoglobulin, were downregulated in mastitic whey. These results indicated significant differences in protein expression between healthy yaks and those with clinical mastitis, and they may provide valuable information for finding new regulation markers and potential protein targets for the treatment of mastitis.

show abstract

Section: Discussionmentioning

confidence: 54%

Comparative proteomic changes of differentially expressed whey proteins in clinical mastitis and healthy yak cows

Li¹,

Ding²,

Wan³

et al. 2014

Genet. Mol. Res.

View full text Add to dashboard Cite

show abstract

“…These peptides have been shown to exhibit a variety of bioactivities, such as antithrombotic, antihypertensive, immunostimulating, and opioidal properties (14). Peptides derived from the milk proteins lactoferrin (1) and ␣ s2 -casein (29) have been shown to exhibit activity against a range of gram-positive and gram-negative bacteria. It has been suggested that the release of these antibacterial peptides upon milk ingestion may assist the developing immune system of the neonate to control the intestinal microflora (1).…”

Section: Discussionmentioning

confidence: 99%

Kappacin, a Novel Antibacterial Peptide from Bovine Milk

Malkoski

Dashper

O'Brien-Simpson

et al. 2001

Antimicrob Agents Chemother

185

141

View full text Add to dashboard Cite

Caseinomacropeptide (CMP) is a heterogeneous C-terminal fragment (residues 106 to 169) of bovine milk -casein composed of glycosylated and phosphorylated forms of different genetic variants. We have demonstrated that CMP has growth-inhibitory activity against the oral opportunistic pathogens Streptococcus mutans and Porphyromonas gingivalis and against Escherichia coli. CMP was fractionated using reversed-phase highperformance liquid chromatography (RP-HPLC), and each fraction was tested for activity against S. mutans in a 96-well-plate broth assay. Fractions were characterized by N-terminal sequence analysis and mass spectrometry. The active form of CMP was shown to be the nonglycosylated, phosphorylated -casein (residues 106 to 169) [-casein(106-169)], which we have designated kappacin. Endoproteinase Glu-C was used to hydrolyze CMP, and the generated peptides were separated using RP-HPLC and gel filtration-HPLC and then tested for activity against S. mutans. The peptide Ser(P) 149 -casein-A(138-158) was the only peptide generated by endoproteinase Glu-C digestion that exhibited growth-inhibitory activity. Peptides corresponding to the sequences of the inhibitory peptide Ser(P) 149 -casein-A(138-158) and its nonphosphorylated counterpartcasein-A(138-158) were chemically synthesized and tested for antibacterial activity. The synthetic Ser(P) 149-casein-A(138-158) displayed growth-inhibitory activity against S. mutans (MIC, 59 g/ml [26 M]). The nonphosphorylated peptide, however, did not inhibit growth at the concentrations tested, indicating that phosphorylation is essential for activity.The caseins are the most abundant bovine milk proteins, and there are four major types: ␣ s1 -, ␣ s2 -, ␤-, and -casein (23). All four caseins are phosphorylated on specific seryl residues, and in addition, -casein is glycosylated (4). -Casein is hydrolyzed by the enzyme chymosin between Phe 105 and Met 106 , generating two polypeptides: a hydrophobic N-terminal para--casein polypeptide -casein (residues 1 to 105) [-casein(1-105)] and a hydrophilic phosphorylated and glycosylated C-terminal polypeptide -casein(106-169), known as the caseinomacropeptide (CMP). CMP is heterogeneous and contains all the posttranslational modification sites (glycosylation and phosphorylation) of -casein. Six potential glycosylation sites have been identified on CMP (18), and up to five different carbohydrate moieties may be attached at each site (20). Three genetic variants of CMP have also been identified, originating from the precursors -casein A, B, and E, with variants A and B being the most common in bovine milk (15).CMP and CMP-derived peptides have been reported to have a variety of biological activities, such as suppression of gastric secretions (28), depression of platelet aggregation (2), inhibition of influenza virus hemagglutination (8), inhibition of cholera toxin binding (9), and immunomodulating activities (14). CMP has also been shown to incorporate into salivary pellicle and inhibit the adherence of Streptococcus mutans, the oral...

show abstract

“…Proteins of food origin and milk proteins in particular have been identified as a rich source of antimicrobial peptides, many of which have been extensively characterized (3). Milk-derived AMPs include caseicins (4), kappacin (5), isracidin (6), lactoferricin (7), casocidin-I (8), and the fragment comprising residues 183 to 207 [f(183-207)] of bovine ␣ s2 -casein (9). The latter was identified in a peptic hydrolysate of bovine ␣ s2 -casein and shows high antibacterial activity against both Gram-positive and Gram-negative bacteria, with MICs in the M range (9,10).…”

mentioning

confidence: 99%

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α _s2 -Casein f(183–207)

Álvarez‐Ordóñez

Begley

Clifford

et al. 2013

Appl Environ Microbiol

View full text Add to dashboard Cite

Casocidin‐I: a casein‐α_s2 derived peptide exhibits antibacterial activity

Cited by 184 publications

References 30 publications

Comparative proteomic changes of differentially expressed whey proteins in clinical mastitis and healthy yak cows

Comparative proteomic changes of differentially expressed whey proteins in clinical mastitis and healthy yak cows

Kappacin, a Novel Antibacterial Peptide from Bovine Milk

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α _s2 -Casein f(183–207)

Contact Info

Product

Resources

About

Casocidin‐I: a casein‐αs2 derived peptide exhibits antibacterial activity

Cited by 184 publications

References 30 publications

Comparative proteomic changes of differentially expressed whey proteins in clinical mastitis and healthy yak cows

Comparative proteomic changes of differentially expressed whey proteins in clinical mastitis and healthy yak cows

Kappacin, a Novel Antibacterial Peptide from Bovine Milk

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α s2 -Casein f(183–207)

Contact Info

Product

Resources

About

Casocidin‐I: a casein‐α_s2 derived peptide exhibits antibacterial activity

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α _s2 -Casein f(183–207)