Lipoprotein(a) Binds to C-terminal Lysine Residues of Recombinant Enolase Derived from Group A <i>Streptococcus</i>

Liping Xu; Wencheng Bai; Zhixing Ji; Xiaoyan Dai; Yun Pang; Feng Huo; Wenlong Li; Runlin Han

doi:doi:10.11648/j.ajcem.20150305.33

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Lipoprotein(a) Binds to C-terminal Lysine Residues of Recombinant Enolase Derived from Group A Streptococcus

Liping Xu, Wencheng Bai, Zhixing Ji, Xiaoyan Dai, Yun Pang, Feng Huo, Wenlong Li, Runlin Han

Published in American Journal of Clinical and Experimental Medicine (Volume 3, Issue 5)

Received: 3 December 2015 Accepted: Published: 4 December 2015

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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.

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), 2024. Published by Science Publishing Group

Keywords

Lipoprotein(a), Group A Streptococcus, Plasminogen, α-Enolase

References

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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

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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

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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

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@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}
}

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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  -

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Author Information

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

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Plain Text BibTeX RIS

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

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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

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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

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@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}
}

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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  -

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