Antimicrobial Peptide AP00205

     
 

APD ID:

AP00205

 
 

Name/Class:

Nisin A (NisaplinTM, ChrisinTM, food additive E234; lantibiotic, type 1, class 1 bacteriocin, Gram-positive bacteria, prokaryotes; XXT5; XXW3; UCSS1b; ZZS; BBW; BBMm; JJsn; Variants: nisin AP)

 
 

Source:

Streptococcus lactis, reclassified as Lactococcus lactis

 
 

Sequence:

ITSISLCTPGCKTGALMGCNMKTATCHCSIHVSK

 
 

Length:

34

 
 

Net charge:

3

 
 

Hydrophobic residue%:

44%

 
 

Boman Index:

0.37 kcal/mol

 
 

3D Structure:

nonhelixbeta

 
 

Method:

NMR

 
 

SwissProt ID:

PDB ID: 1WCO   Go to PDB

 
 

Activity:

Anti-Gram+, Spermicidal, Antibiofilm, Wound healing, Anticancer

 
 

Crucial residues:

The thioether bonds and the hinge region are essential for activity. Oxidation of the sulfur made the peptide inactive (Wilson-Stanford, S et al. 2009 Appl Environ Microbiol 75: 1381-1387).

 
 

Additional info:

Antimicrobial activity: Bacterial inhibitory activity was first reported in 1928. Active against Micrococcus spp. (MIC 1.1 ug/ml), Enterococcus spp. (MIC 16.7), Listeria spp., Staphylococcus spp., Streptococcus spp., Bacillus spp. (MIC 4.2-8.4), Clostridium spp. (MIC 1.1), A. viscosus (MIC 83.6 ug/ml), Peptostreptococcus spp., C. diphtheriae, G. vaginalis, M. smegmatis, P. acnes (MIC 2.1-8.4 ug/ml) (Ref see AP1003), and Gram- bacteria: C. jejune (MIC 1.1 ug/ml), H. influenzae (MIC 66.9), H. pylori (MIC 0.3), and Neisseria spp (MIC 8.4). It also has spermicidal effect. Nisin showed synergistic effect with lactoferrin against foodborne pathogens such as L monocytogenes and E. coli O157:H7 (Murdock CA et al 2007 Lett Appl Microbiol 44: 255-61). It also has antibiofilmB activity against S. mutans (Tong Z et al., 2011).

Post-translational modification. Shown is the amino acid sequence derived from nucleotide and the actual active form is a translationally modified peptide. There are two di-hydroalanines (Dha): S5 and S33; one di-dehydrobutyrine (Dhb): T2; one lanthionine: S3-C7; and four methyllanthionines: T8-C11, T13-C19, T23-C26, and T25-C28 (Gross E, Morell JL 1971 J Am Chem Soc 93: 4634) (Provided by Torsten Stein).

Structure: For NMR structural studies in SDS and DPC, see Van den Hooven HW et al. 1996. Eur J Biochem 235: 382. You can rotate, zoom, and view the 3D structure in complex lipid II here in the PDB .

MOA: dual mechanism, i.e. the peptide binds to lipid II followed by forming a pore on the membranes (Science 2006; 313: 1636-1637).

Engineering: Importantly, recent work reveals that the enzymes (NisBTC) responsible for nisin generation may be applied to the modification of other peptides, potentially to improve the protease stability of the template.

AMPs in use: Nisin is a food preservative in use in more than 80 countries (approved by the European Union in 1983 and FDA in 1988). Swiss-Prot P13068. Nisin AP, a high content form (95%), can inhibit head and Neck Cancer tumorigenesis (Kamarajan et al., 2015). Nisin has also been covalently immobilized 2011Qi et al. to a multiwalled carbon nanotube. Edited 11/2011; 4/2014; 7/2015; 10/2015; 7/2016; 12/2016; 10/2017, GW.

 
       
 

Title:

The inhibiting effect of Streptococcus lactis on Lactobacillus bulgaricus.

 
 

Author:

Rogers, LA1928

 
 

Reference:

J. Bacteriol. 1928; 16:321-325. PubMed.

 
       

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