Molecular cloning and characterization of Taiwan macaque lactoferrin.
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).


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.
Chang
Jui-Hsien
JH
Department of Parasitology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Chen
Chao-Chung
CC
Chao
Ming-Chieh
MC
Chuang
Yin-Ching
YC
Chang
Ming-Chung
MC