AI Article Synopsis
- Lactoferrin (LF) is a glycoprotein that helps protect mammals against pathogens and is responsible for binding iron.
- Researchers cloned and sequenced the cDNA for LF from Taiwan macaque to analyze its properties.
- The study found that macaque LF is highly similar to both rhesus monkey LF and human LF, showing comparable antibacterial abilities and similar iron release patterns, with slight differences in activity against specific bacteria.
Article Abstract
Background: Lactoferrin (LF) is an iron-binding glycoprotein that plays an important role in combating a wide range of pathogens and contributes innate protective defenses of mammals.
Methods: We cloned and sequenced the full-length cDNA for LF from Taiwan macaque. The antimicrobial activity and iron-binding ability of the purified recombinant macaque LF (rmLF) were determined and compared with those of human LF (hLF).
Results And Conclusions: The complete mLF cDNA (GenBank: EU523857) encoded a 710-aa precursor with a 19-aa signal peptide. The nucleotide sequence of mLF showed the highest identity to the rhesus monkey LF (98%), whereas the putative amino acid sequence of mLF showed the highest identity to the hLF (90%). The rmLF and natural hLF showed almost equivalent antibacterial activities against Klebsiella pneumoniae and mLF presented a slightly lower activity against Listeria monocytogenes than natural hLF. In addition, the patterns of iron release from mLF and hLF were nearly identical.
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| http://dx.doi.org/10.1111/j.1600-0684.2008.00318.x | DOI Listing |
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