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.
Published in | American Journal of Clinical and Experimental Medicine (Volume 3, Issue 5) |
DOI | 10.11648/j.ajcem.20150305.33 |
Page(s) | 327-331 |
Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
Copyright |
Copyright © The Author(s), 2015. Published by Science Publishing Group |
Lipoprotein(a), Group A Streptococcus, Plasminogen, α-Enolase
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APA Style
Liping Xu, Wencheng Bai, Zhixing Ji, Xiaoyan Dai, Yun Pang, et al. (2015). Lipoprotein(a) Binds to C-terminal Lysine Residues of Recombinant Enolase Derived from Group A Streptococcus. American Journal of Clinical and Experimental Medicine, 3(5), 327-331. https://doi.org/10.11648/j.ajcem.20150305.33
ACS Style
Liping Xu; Wencheng Bai; Zhixing Ji; Xiaoyan Dai; Yun Pang, et al. Lipoprotein(a) Binds to C-terminal Lysine Residues of Recombinant Enolase Derived from Group A Streptococcus. Am. J. Clin. Exp. Med. 2015, 3(5), 327-331. doi: 10.11648/j.ajcem.20150305.33
AMA Style
Liping Xu, Wencheng Bai, Zhixing Ji, Xiaoyan Dai, Yun Pang, et al. Lipoprotein(a) Binds to C-terminal Lysine Residues of Recombinant Enolase Derived from Group A Streptococcus. Am J Clin Exp Med. 2015;3(5):327-331. doi: 10.11648/j.ajcem.20150305.33
@article{10.11648/j.ajcem.20150305.33, author = {Liping Xu and Wencheng Bai and Zhixing Ji and Xiaoyan Dai and Yun Pang and Feng Huo and Wenlong Li and Runlin Han}, title = {Lipoprotein(a) Binds to C-terminal Lysine Residues of Recombinant Enolase Derived from Group A Streptococcus}, journal = {American Journal of Clinical and Experimental Medicine}, volume = {3}, number = {5}, pages = {327-331}, doi = {10.11648/j.ajcem.20150305.33}, url = {https://doi.org/10.11648/j.ajcem.20150305.33}, eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajcem.20150305.33}, abstract = {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.}, year = {2015} }
TY - JOUR T1 - Lipoprotein(a) Binds to C-terminal Lysine Residues of Recombinant Enolase Derived from Group A Streptococcus AU - Liping Xu AU - Wencheng Bai AU - Zhixing Ji AU - Xiaoyan Dai AU - Yun Pang AU - Feng Huo AU - Wenlong Li AU - Runlin Han Y1 - 2015/12/04 PY - 2015 N1 - https://doi.org/10.11648/j.ajcem.20150305.33 DO - 10.11648/j.ajcem.20150305.33 T2 - American Journal of Clinical and Experimental Medicine JF - American Journal of Clinical and Experimental Medicine JO - American Journal of Clinical and Experimental Medicine SP - 327 EP - 331 PB - Science Publishing Group SN - 2330-8133 UR - https://doi.org/10.11648/j.ajcem.20150305.33 AB - 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. VL - 3 IS - 5 ER -