Lipoprotein(a) Binds to C-terminal Lysine Residues of Recombinant Enolase Derived from Group A Streptococcus
American Journal of Clinical and Experimental Medicine
Volume 3, Issue 5, September 2015, Pages: 327-331
Received: Dec. 3, 2015;
Published: Dec. 4, 2015
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Liping Xu, Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China; College of Basic Medicine, Inner Mongolia Medical University, Huhhot, China
Wencheng Bai, Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China
Zhixing Ji, Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China; Jining No. 1 Middle school, Jining, China
Xiaoyan Dai, Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China; Tianjin Institute of Scientific and Technical Information, Tianjin, China
Yun Pang, Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China; Inner Mongolia Yili Industrial Group Co., Ltd, Huhhot, China
Feng Huo, College of Life Science, Inner Mongolia Agricultural University, Huhhot, China
Wenlong Li, Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China
Runlin Han, Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China
The biological function of lipoprotein(a) [Lp(a)] remains elusive although it was identified in 1963. We previously hypothesized that Lp(a) might inhibit pathogens from hijacking host plasminogen (Plg) since apolipoprotein(a) [Apo(a)], a unique protein in Lp(a), shares a high homology with Plg. We demonstrate that Lp(a) bound to recombinant Streptococcal α-enolase (rSEN), which is a surface Plg receptor on group A Streptococcus (GAS). However, recombinant C-terminal lysines-deleted variant of enolase (rSENΔ434-435) did not bind to Lp(a). Moreover, epsilon-aminocaproic acid (EACA), a lysine analog, significantly inhibited the binding of rSEN to Lp(a). Collectively, Lp(a) via its LBS bound to the C-terminal lysines of rSEN. In addition, Lp(a) only competitively blocked the Plg-rSEN interaction but not Plg-rSENΔ434-435 interaction since Plg could also bind to the internal lysine residue of α-enolase. The preliminary study indicated that Lp(a) also interacted with GAS, consequently competitively inhibiting the Plg-GAS binding to some extent. Therefore, Lp(a) might play a limited role in preventing GAS infection since it only partially inhibited the pathogen from recruiting host Plg.
Lipoprotein(a) Binds to C-terminal Lysine Residues of Recombinant Enolase Derived from Group A Streptococcus, American Journal of Clinical and Experimental Medicine.
Vol. 3, No. 5,
2015, pp. 327-331.
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