Antimicrobial Peptide AP02257

     
 

APD ID:

AP02257

 
 

Name/Class:

Lysozyme (lectin-binding enzyme, human, primates, mammals, animals; BBS; JJsn; UCSS1a)

 
 

Source:

Secretions and Tissues, tears, saliva, human milk, and mucus; Homo sapiens

 
 

Sequence:

KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV

 
 

Length:

130

 
 

Net charge:

8

 
 

Hydrophobic residue%:

40%

 
 

Boman Index:

2.28 kcal/mol

 
 

3D Structure:

Combine Helix and Beta structure

 
 

Method:

X-ray

 
 

SwissProt ID:

PDB ID: 3FE0   Go to PDB

 
 

Activity:

Anti-Gram+ & Gram-, Antifungal,

 
 

Crucial residues:

 
 

Additional info:

Both Professors Robert Lehrer and Richard Gallo pointed at lysozyme as the first antimicrobial peptide (see AMP discovery timeline). And the classic paper in the ref is recommended by Dr. Gallo as the beginning (birth) of modern innate immunity. The structure and activity relationship of human lysozyme can be found in modern Biochemistry textbooks. It catalytically hydrolyzes bacterial cell wall peptidoglycan and has also been shown to exert catalysis-independent antimicrobial properties, thereby active against both Gram-positive and -negative bacteria. You can rotate, zoom, and view the crystal structure here in the PDB. It showed synergistic effect with LL-37 (Abou Aliwa et al., 2014).

Pathogen infection strategy: Mycobacterium tuberculosis uses a novel glycosylated and surface-localized lipoprotein, LprI, to abrogate the lytic activity of lysozyme (Sethi D eta l., 2016). Updated 2/2016; Jan2017 GW.

 
       
 

Title:

Observations on a Bacteriolytic Substance (“Lysozyme”) Found in Secretions and Tissues

 
 

Author:

Fleming A, Allison VD.1922

 
 

Reference:

Br J Exp Pathol. 1922 October; 3(5): 252–260. Pub-Med Central.

 
       

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