Lipoprotein(a) Binds to Recombinant Nontypeable <i>Haemophilus influenzae</i> Aspartase

Wenlong Li; Liping Xu; Yakun Zhang; Wencheng Bai; Lulei Zhou; Yuxin Li; Na Liu; Ling Liu; Runlin Han

doi:doi:10.11648/j.ajcem.20150305.31

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Lipoprotein(a) Binds to Recombinant Nontypeable Haemophilus influenzae Aspartase

Wenlong Li, Liping Xu, Yakun Zhang, Wencheng Bai, Lulei Zhou, Yuxin Li, Na Liu, Ling Liu, Runlin Han

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

Received: 3 December 2015 Published: 4 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.

Published in	American Journal of Clinical and Experimental Medicine (Volume 3, Issue 5)
DOI	10.11648/j.ajcem.20150305.31
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), 2015. Published by Science Publishing Group

Keywords

Lipoprotein(a), Apolipoprotein(a), Nontypeable Haemophilus influenzae, Plasminogen, Recombinant Aspartase

References

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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://article.sciencepublishinggroup.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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Author Information

Wenlong Li

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

College of Basic Medicine, Inner Mongolia Medical University, Huhhot, China
Yakun Zhang

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

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

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

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

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

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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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://article.sciencepublishinggroup.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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