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; XXO; 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 (XXO) 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.

Production: Phthalyl Starch Nanoparticles as Prebiotics Enhanced Nisin Production in Lactococcus Lactis Through the Induction of Mild Stress in Probiotics (Hong et al., 2020).

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, 6/2020 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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