Details of Host Immune Factor (HIF) Regulating Microbe Species (MIC)

General Information of HIF (ID: HIFM0237)
HIF Name
Human lactoferricin
HIF Synonym(s)
Lactotransferrin, Human lactoferricin, Lactotransferrin, Growth-inhibiting protein 12, Talalactoferrin
HIF Classification
Antimicrobial peptide (AMP)
Molecular Function
Antibiotic; Antimicrobial; DNA-binding; Heparin-binding; Hydrolase; Protease; Serine protease
Description Human lactoferricin has been identified in humans. It forms the first line of host defense against pathogenic infections and are a key component of the ancient innate immune system. [1]
Pfam Transferrin (PF00405 )
Sequence Click here to download the HIF sequence in FASTA format
External Links
Uniprot ID
TRFL_HUMAN
APD ID
AP00763
Microbe Species (MIC) Regulated by This HIF
         Bifidobacterium bifidum (actinobacteria) MIC00209
             Description Human LF (lactoferrin) may have activity to Bifidobacterium bifidum. [2]
         Escherichia coli (enterobacteria) MIC00516
             Description Lactoferricin has shown antibacterial activity against enterotoxigenic Escherichia coli. [3]
         Glaesserella parasuis (gamma-proteobacteria) MIC00654
             Description Human milk lactoferrin is a serine protease that could cleave Haemophilus surface proteins at arginine-rich sites. [4]
         Lactobacillus sp. (firmicutes) MIC00701
             Description A positive correlation between the fecal Lactobacillus amount and lactoferrin has previously been reported in 3-day old infants. [5]
         Listeria monocytogenes (firmicutes) MIC00771
             Description Lactoferricin has shown antibacterial activity against enterotoxigenic Listeria monocytogenes. [3]
References
1 APD: the Antimicrobial Peptide Database.Nucleic Acids Res. 2004 Jan 1;32(Database issue):D590-2. doi: 10.1093/nar/gkh025.
2 Lactoferrin and bifidobacteria.Biometals. 2014 Oct;27(5):915-22. doi: 10.1007/s10534-014-9741-8. Epub 2014 Apr 27.
3 Not Avaliable
4 Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites.Mol Microbiol. 2003 Feb;47(3):607-17. doi: 10.1046/j.1365-2958.2003.03327.x.
5 Not Avaliable

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