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The Interaction between Plasma Lipoprotein(a) and Recombinant Protein E Derived from Nontypeable Haemophilus influenza |
Yu WANG1,4,Zhi LIU1,4,Wen-cheng BAI2,4,Li-ping XU3,Run-lin HAN2,4() |
1 College of Life Science, Inner Mongolia Agriculture University, Hohhot 010018, China 2 College of Veterinary Medicine, Inner Mongolia Agriculture University, Hohhot 010018, China 3 College of Basic Medicine, Inner Mongolia Medical University, Hohhot 010018, China 4 Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agriculture University, Hohhot 010018, China |
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Abstract Objective:Protein E (PE), with two lysine residues at its C-terminus, is a plasminogen (Plg) receptor on the surface of nontypeable Haemophilus influenza (NTHi). NTHi can recruit Plg on the cell surface by PE and utilize host fibrinolytic system to achieve its immune invasion. Based on the high homology of Plg and Apolipoprotein(a) [Apo(a)] of Lipoprotein(a) [Lp(a)], Lp(a) was supposed to bind to PE. Methods:The recombinant PE (rPE) and C-terminal lysine residues-deleted variant (rPEΔKK) were obtained by prokaryotic expression and further purified. Lp(a) was isolated and purified from human plasma by KBr density gradient centrifugation followed by Q SepharoseTM Fast Flow ion exchange chromatography. The interaction between rPE and Lp(a) was investigated by enzyme-linked immunosorbent assay(ELISA) and Pull down followed by Western blot. Results:The results indicated that rPE could bind to Lp(a) but not to LDL, and the interaction was significantly inhibited by EACA. The binding capacity of rPEΔKK to Lp(a) was obviously lower than that of rPE. In addition, Lp(a) could inhibit the binding of rPE to Plg slightly. Conclusion:In overall, Lp(a) could bind to rPE and the C-terminal lysine residues of rPE and the lysine binding site(LBS) of Apo(a) was responsible for this interaction.
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Received: 15 August 2017
Published: 16 December 2017
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