Part:BBa_K1742007
Homo sapiens LTF Lactoferrin
Natural response to infection in the lower respiratory tract depends mainly in the neutrophilic granulocyte which secret several products in order to fight infection. One of these products is lactoferrin, a glicosilated protein with two homologous domains able to interact with iron ions. It is the chelating property the one which gives this protein their bacteriostatic activity [1]. The bactericidal activity resides in the N-lobe of the protein, it acts agains E.coli or V.cholerae among others. Oral administrationof lactoferrin has been prove to has antimicrobial but also antiviral activity in animals models [2] increasing the levels of leukocytes and cytokines as interferon gamma, interleukin 12 and 18. It also stimulates the activity of macrophages, so lactoferrin plays an important role in pathogen eradication and homeostasis maintenance in episodes of infection.
Pneumonia major cause is the infection by Streptococcus pneumoniae, causing also meningitis, septicemia and otitis media [3]. Mirza Shaper et al, 2004[4], observed that lactoferrin apoprotein (without iron ions) has bactericidal activity. They also confirmed that this activity is maintained by just the first 11 amino acids of the N-terminous domain.
MIT_MAHE 2020
Summary
Natural response to infection in the lower respiratory tract depends mainly in the neutrophilic granulocyte which secret several products in order to fight infection. One of these products is lactoferrin, a glicosilated protein with two homologous domains able to interact with iron ions. It is the chelating property the one which gives this protein their bacteriostatic activity. Oral administrationof lactoferrin has been prove to has antimicrobial but also antiviral activity in animals models increasing the levels of leukocytes and cytokines as interferon gamma, interleukin 12 and 18. It also stimulates the activity of macrophages, so lactoferrin plays an important role in pathogen eradication and homeostasis maintenance in episodes of infection.
References
1. Otto BR, Verweij-van Vaught AM, MacLaren DM (1992). Transferrins and Heme-Compounds as Iron Sources for Pathogenic Bacteria. Critical Reviews in Microbiology, 18(3): 217-233
2. Teraguchi S, Wakabayashi H, Kuwata H, Yamauchi K, Tamura Y (2004). Protection against infections by oral lactoferrin: Evaluation in animal models. Biometals: an international journal on the role of metal ions in biology, biochemistry and medicine, 17(3): 231-234
3. Butler JC, Schuchat A (1999) Epidemology of pneumococcal infections in the elderly, Drugs & aging, 15 Suppl 1:11-9
4. Mirza S, Hollingshead SK, Benjamin WH, Briles DE (2004). PspA protects Streptococcus pneumonia from Killing by Apolactoferrin, and Antibody to PspA Enhances Killing of Pneumococci by Apolactoferrin. Infection and Immunity, 72(12):7379
5. Shaper, M., Hollingshead, S. K., Benjamin, W. H., Jr, & Briles, D. E. (2004). PspA protects Streptococcus pneumoniae from killing by apolactoferrin, and antibody to PspA enhances killing of pneumococci by apolactoferrin [corrected]. Infection and immunity, 72(9), 5031–5040. https://doi.org/10.1128/IAI.72.9.5031-5040.2004
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 891
Illegal BglII site found at 1501 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI site found at 1428
//collections/immune_regulation/inflammatory
| None |