American Journal of Clinical and Experimental Medicine

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Lipoprotein(a) Binds to Recombinant Nontypeable Haemophilus influenzae Aspartase

Received: 03 December 2015    Accepted:     Published: 04 December 2015
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Abstract

The respiratory pathogen nontypeable Haemophilus influenza (NTHi) can recruit plasminogen (Plg) on the cell surface by its Plg receptor aspartase (ASP) and utilize host Plg and fibrinolytic system to achieve its adherence and immune invasion. Lipoprotein(a) [Lp(a)] consists of one molecule low-density lipoprotein (LDL) and one molecule apolipoprotein(a) [Apo(a)]. Apo(a) shares a high degree of homology with the human Plg, and both of them contain lysine-binding sites (LBS), which enables them to interact with various cell-surface receptors or fibrin(ogen). However, the definite physiological function of Lp(a) remains vague. Here, we present evidence that Lp(a) via its Apo(a) may bind to thePlg receptor ASP. Recombinant aspartase (rASP) and C-terminal lysine-deleted variant of ASP (rASPΔK) were used in the current study. The rASP specifically bound to Lp(a), but rASPΔK did not, indicating that C-terminal lysine residue of rASP was responsible for the interaction. In addition, rASP interacted with Lp(a), but not with LDL, revealing that LBS of Apo(a) was involved in the binding. Our results also showed that Lp(a) could inhibit the binding of Plg to rASP. Plasma Lp(a) might play a role in anti-NTHi infection by binding to its Plg receptor ASP.

DOI 10.11648/j.ajcem.20150305.31
Published in American Journal of Clinical and Experimental Medicine (Volume 3, Issue 5, September 2015)
Page(s) 314-321
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), Apolipoprotein(a), Nontypeable Haemophilus influenzae, Plasminogen, Recombinant Aspartase

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

  • Research Center of Plasma Lipoprotein Immunology, 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

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

  • Research Center of Plasma Lipoprotein Immunology, Inner Mongolia Agricultural University, Huhhot, China; Key Laboratory of Animal Clinic Diagnosis and Treatment (Ministry of Agriculture of the People’s Republic of China), Inner Mongolia Agricultural University, Huhhot, China

Cite This Article
  • APA Style

    Wenlong Li, Liping Xu, Yakun Zhang, Wencheng Bai, Lulei Zhou, et al. (2015). Lipoprotein(a) Binds to Recombinant Nontypeable Haemophilus influenzae Aspartase. American Journal of Clinical and Experimental Medicine, 3(5), 314-321. https://doi.org/10.11648/j.ajcem.20150305.31

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    ACS Style

    Wenlong Li; Liping Xu; Yakun Zhang; Wencheng Bai; Lulei Zhou, et al. Lipoprotein(a) Binds to Recombinant Nontypeable Haemophilus influenzae Aspartase. Am. J. Clin. Exp. Med. 2015, 3(5), 314-321. doi: 10.11648/j.ajcem.20150305.31

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    AMA Style

    Wenlong Li, Liping Xu, Yakun Zhang, Wencheng Bai, Lulei Zhou, et al. Lipoprotein(a) Binds to Recombinant Nontypeable Haemophilus influenzae Aspartase. Am J Clin Exp Med. 2015;3(5):314-321. doi: 10.11648/j.ajcem.20150305.31

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  • @article{10.11648/j.ajcem.20150305.31,
      author = {Wenlong Li and Liping Xu and Yakun Zhang and Wencheng Bai and Lulei Zhou and Yuxin Li and Na Liu and Ling Liu and Runlin Han},
      title = {Lipoprotein(a) Binds to Recombinant Nontypeable Haemophilus influenzae Aspartase},
      journal = {American Journal of Clinical and Experimental Medicine},
      volume = {3},
      number = {5},
      pages = {314-321},
      doi = {10.11648/j.ajcem.20150305.31},
      url = {https://doi.org/10.11648/j.ajcem.20150305.31},
      eprint = {https://download.sciencepg.com/pdf/10.11648.j.ajcem.20150305.31},
      abstract = {The respiratory pathogen nontypeable Haemophilus influenza (NTHi) can recruit plasminogen (Plg) on the cell surface by its Plg receptor aspartase (ASP) and utilize host Plg and fibrinolytic system to achieve its adherence and immune invasion. Lipoprotein(a) [Lp(a)] consists of one molecule low-density lipoprotein (LDL) and one molecule apolipoprotein(a) [Apo(a)]. Apo(a) shares a high degree of homology with the human Plg, and both of them contain lysine-binding sites (LBS), which enables them to interact with various cell-surface receptors or fibrin(ogen). However, the definite physiological function of Lp(a) remains vague. Here, we present evidence that Lp(a) via its Apo(a) may bind to thePlg receptor ASP. Recombinant aspartase (rASP) and C-terminal lysine-deleted variant of ASP (rASPΔK) were used in the current study. The rASP specifically bound to Lp(a), but rASPΔK did not, indicating that C-terminal lysine residue of rASP was responsible for the interaction. In addition, rASP interacted with Lp(a), but not with LDL, revealing that LBS of Apo(a) was involved in the binding. Our results also showed that Lp(a) could inhibit the binding of Plg to rASP. Plasma Lp(a) might play a role in anti-NTHi infection by binding to its Plg receptor ASP.},
     year = {2015}
    }
    

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  • TY  - JOUR
    T1  - Lipoprotein(a) Binds to Recombinant Nontypeable Haemophilus influenzae Aspartase
    AU  - Wenlong Li
    AU  - Liping Xu
    AU  - Yakun Zhang
    AU  - Wencheng Bai
    AU  - Lulei Zhou
    AU  - Yuxin Li
    AU  - Na Liu
    AU  - Ling Liu
    AU  - Runlin Han
    Y1  - 2015/12/04
    PY  - 2015
    N1  - https://doi.org/10.11648/j.ajcem.20150305.31
    DO  - 10.11648/j.ajcem.20150305.31
    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  - 314
    EP  - 321
    PB  - Science Publishing Group
    SN  - 2330-8133
    UR  - https://doi.org/10.11648/j.ajcem.20150305.31
    AB  - The respiratory pathogen nontypeable Haemophilus influenza (NTHi) can recruit plasminogen (Plg) on the cell surface by its Plg receptor aspartase (ASP) and utilize host Plg and fibrinolytic system to achieve its adherence and immune invasion. Lipoprotein(a) [Lp(a)] consists of one molecule low-density lipoprotein (LDL) and one molecule apolipoprotein(a) [Apo(a)]. Apo(a) shares a high degree of homology with the human Plg, and both of them contain lysine-binding sites (LBS), which enables them to interact with various cell-surface receptors or fibrin(ogen). However, the definite physiological function of Lp(a) remains vague. Here, we present evidence that Lp(a) via its Apo(a) may bind to thePlg receptor ASP. Recombinant aspartase (rASP) and C-terminal lysine-deleted variant of ASP (rASPΔK) were used in the current study. The rASP specifically bound to Lp(a), but rASPΔK did not, indicating that C-terminal lysine residue of rASP was responsible for the interaction. In addition, rASP interacted with Lp(a), but not with LDL, revealing that LBS of Apo(a) was involved in the binding. Our results also showed that Lp(a) could inhibit the binding of Plg to rASP. Plasma Lp(a) might play a role in anti-NTHi infection by binding to its Plg receptor ASP.
    VL  - 3
    IS  - 5
    ER  - 

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