American Journal of Clinical and Experimental Medicine

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

Received: 03 December 2015    Accepted:     Published: 04 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.

DOI 10.11648/j.ajcem.20150305.33
Published in American Journal of Clinical and Experimental Medicine (Volume 3, Issue 5, September 2015)
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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Author Information
  • Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China; College of Basic Medicine, Inner Mongolia Medical University, Huhhot, China

  • Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China

  • Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China; Jining No. 1 Middle school, Jining, China

  • Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China; Tianjin Institute of Scientific and Technical Information, Tianjin, China

  • Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China; Inner Mongolia Yili Industrial Group Co., Ltd, Huhhot, China

  • College of Life Science, Inner Mongolia Agricultural University, Huhhot, China

  • Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China

  • Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China

Cite This Article
  • 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://download.sciencepg.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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