The Interaction Between Recombinant Protein F Derived from Nontypeable <i>Haemophilus influenza</i> and Lipoprotein(a)

Liu En; Li Weng-long; Han Run-lin

doi:doi:10.11648/j.ajcem.20150306.11

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The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a)

Liu En, Li Weng-long, Han Run-lin

Published in American Journal of Clinical and Experimental Medicine (Volume 3, Issue 6)

Received: 3 December 2015 Published: 5 December 2015

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Abstract

Protein F (PF) is a surface plasminogen (Plg) receptor on the nontypeable Haemophilus influenza (NTHi). Plg via its lysine binding sites (LBS) can bind to PF. Apolipoprotein(a) [Apo(a)] is one component of Lipoprotein(a) [Lp(a)]. It has Kringle (K) domains, which contain LBS and has a high homology with Plg. Therefore, we speculated that Lp(a) might bind to Plg receptor on the surface of NTHi, subsequently competitively inhibiting the interaction of NTHi with Plg. In this study, recombinant PF (rPF) and its C-terminal lysine residue-deleted variant (rPFΔK) were expressed in E. coli BL21. The interactions of rPF with Plg and Lp(a) were tested by ELISA. The results showed that rPF could bind to Plg and Lp(a). The binding capacity of rPF was significantly higher than that of rPFΔK. The interactions of rPF with Plg and Lp(a) could be inhibited by EACA. 2 mmol/L of EACA significantly inhibited the binding of rPF to Plg, while 0.2 mmol/L of EACA could significantly reduce the binding of rPF to Lp(a). 50 ng/100 μL Lp(a) could significantly inhibit the interaction of rPF with Plg. In addition, affinity chromatography assay followed by Western biotting was also used to study the interaction. In overall, C-terminal lysine residue of rPF and the lysine binding sites (LBS) of Plg and Lp(a) should be responsible for these specifically bindings. Lp(a) could combine with rPF consequently inhibiting the interaction of Plg with rPF. This revealed that Lp(a) might play a role in anti-NTHi infection.

Published in	American Journal of Clinical and Experimental Medicine (Volume 3, Issue 6)
DOI	10.11648/j.ajcem.20150306.11
Page(s)	338-343
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

Nontypeable Haemophilus Influenzae, Plasminogen, Lipoprotein(a), Recombinant Protein F

References

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[2]	Morris SK. Moss WJ, Halesa N, et al. Haemophilus influenzae type b conjugate vaccine use and effectiveness[J].Lancet Infectious Diseases, 2008, 8(7); 435–443.
[3]	Erwin AL, Smith AL. Nontypeable Haemophilus influenzae: understanding virulence and commensal behavior[J]. Trends Microbiol, 2007, 15(8); 355–362.
[4]	Murphy TF, Faden H, Bakaletz LO, et al. Nontypeable Haemophilus influenzae as a pathogen in children[J]. Pediatric Infectious Diseases, 2009, 28(1); 43–48.
[5]	Turk DC. The pathogenicity of Haemophilus influenzae[J]. J Med Microbiol, 1984, 18:1–16.
[6]	Lahteenmaki K, Kuusela P, Korhonen TK. Bacterial plasminogen activators and receptor[J]. FEMS Microbiology Reviews, 2001, 25(5):531-552.
[7]	Redlitz A, Plow EF. Receptors for plasminogen and t-PA: an update[J]. Baillieres Clinical Haematology, 1995, 8(2):313-327.
[8]	Barthel D, Singh B, Riesbeck K, et al. Haemophilus influenzae uses the surface protein E to acquire human plasminogen and to evade innate immunity[J]. Immunology, 2012, 188(1); 379-385.
[9]	Sjostrom I, Grondahl H, Falk G, et al. Purification and characterisation of a plasminogen-binding protein from Haemophilus influenzae. Sequence determination reveals identity with aspartase[J]. Biochimica et Biophysica Acta, 1997, 1324(2); 182–190.
[10]	Su YC, Mukherjee O, Singh B, et al. Haemophilus influenza P4 interacts with extracellular matrix proteins promoting adhesion and serum resistance[Z]. http://jid.oxfordjournals.org, 2015-8-7.
[11]	Jalalvand F, Su YC, Mörgelin M, et al. Haemophilus influenzae protein F mediates binding to laminin and human pulmonary epithelial cells[J]. Infectious Diseases, 2013, 207(5); 803-813.
[12]	Su YC, Jalalvand F, Mörgelin M, et al. Haemophilus influenza acquires vitronectin via the ubiquitous protein F to subvert host innate immunity[J]. Molecular Microbiology, 2013, 87 (6); 1245–1266.
[13]	Han RL. Plasma lipoproteins are important components of the immune system[J]. Microbiol Immunol. 2010, 54 (4); 246-253.
[14]	Boeryd B. Action of heparin and plasminogen inhibitor (EACA) on metastatic tumour spread in an isologous system[J]. Acta pathologica et microbiologica Scandinavica. 1965, 65(3):395-404.
[15]	Mclean JW, Tomlinson JE, Kuang WJ, et al. cDNA secquence of human apolipoprotein(a) is homologous to plasminogen[J]. Nature, 1987, 330(6144):132-137.

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APA Style

Liu En, Li Weng-long, Han Run-lin. (2015). The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a). American Journal of Clinical and Experimental Medicine, 3(6), 338-343. https://doi.org/10.11648/j.ajcem.20150306.11

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ACS Style

Liu En; Li Weng-long; Han Run-lin. The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a). Am. J. Clin. Exp. Med. 2015, 3(6), 338-343. doi: 10.11648/j.ajcem.20150306.11

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AMA Style

Liu En, Li Weng-long, Han Run-lin. The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a). Am J Clin Exp Med. 2015;3(6):338-343. doi: 10.11648/j.ajcem.20150306.11

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@article{10.11648/j.ajcem.20150306.11,
  author = {Liu En and Li Weng-long and Han Run-lin},
  title = {The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a)},
  journal = {American Journal of Clinical and Experimental Medicine},
  volume = {3},
  number = {6},
  pages = {338-343},
  doi = {10.11648/j.ajcem.20150306.11},
  url = {https://doi.org/10.11648/j.ajcem.20150306.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajcem.20150306.11},
  abstract = {Protein F (PF) is a surface plasminogen (Plg) receptor on the nontypeable Haemophilus influenza (NTHi). Plg via its lysine binding sites (LBS) can bind to PF. Apolipoprotein(a) [Apo(a)] is one component of Lipoprotein(a) [Lp(a)]. It has Kringle (K) domains, which contain LBS and has a high homology with Plg. Therefore, we speculated that Lp(a) might bind to Plg receptor on the surface of NTHi, subsequently competitively inhibiting the interaction of NTHi with Plg. In this study, recombinant PF (rPF) and its C-terminal lysine residue-deleted variant (rPFΔK) were expressed in E. coli BL21. The interactions of rPF with Plg and Lp(a) were tested by ELISA. The results showed that rPF could bind to Plg and Lp(a). The binding capacity of rPF was significantly higher than that of rPFΔK. The interactions of rPF with Plg and Lp(a) could be inhibited by EACA. 2 mmol/L of EACA significantly inhibited the binding of rPF to Plg, while 0.2 mmol/L of EACA could significantly reduce the binding of rPF to Lp(a). 50 ng/100 μL Lp(a) could significantly inhibit the interaction of rPF with Plg. In addition, affinity chromatography assay followed by Western biotting was also used to study the interaction. In overall, C-terminal lysine residue of rPF and the lysine binding sites (LBS) of Plg and Lp(a) should be responsible for these specifically bindings. Lp(a) could combine with rPF consequently inhibiting the interaction of Plg with rPF. This revealed that Lp(a) might play a role in anti-NTHi infection.},
 year = {2015}
}

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TY  - JOUR
T1  - The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a)
AU  - Liu En
AU  - Li Weng-long
AU  - Han Run-lin
Y1  - 2015/12/05
PY  - 2015
N1  - https://doi.org/10.11648/j.ajcem.20150306.11
DO  - 10.11648/j.ajcem.20150306.11
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  - 338
EP  - 343
PB  - Science Publishing Group
SN  - 2330-8133
UR  - https://doi.org/10.11648/j.ajcem.20150306.11
AB  - Protein F (PF) is a surface plasminogen (Plg) receptor on the nontypeable Haemophilus influenza (NTHi). Plg via its lysine binding sites (LBS) can bind to PF. Apolipoprotein(a) [Apo(a)] is one component of Lipoprotein(a) [Lp(a)]. It has Kringle (K) domains, which contain LBS and has a high homology with Plg. Therefore, we speculated that Lp(a) might bind to Plg receptor on the surface of NTHi, subsequently competitively inhibiting the interaction of NTHi with Plg. In this study, recombinant PF (rPF) and its C-terminal lysine residue-deleted variant (rPFΔK) were expressed in E. coli BL21. The interactions of rPF with Plg and Lp(a) were tested by ELISA. The results showed that rPF could bind to Plg and Lp(a). The binding capacity of rPF was significantly higher than that of rPFΔK. The interactions of rPF with Plg and Lp(a) could be inhibited by EACA. 2 mmol/L of EACA significantly inhibited the binding of rPF to Plg, while 0.2 mmol/L of EACA could significantly reduce the binding of rPF to Lp(a). 50 ng/100 μL Lp(a) could significantly inhibit the interaction of rPF with Plg. In addition, affinity chromatography assay followed by Western biotting was also used to study the interaction. In overall, C-terminal lysine residue of rPF and the lysine binding sites (LBS) of Plg and Lp(a) should be responsible for these specifically bindings. Lp(a) could combine with rPF consequently inhibiting the interaction of Plg with rPF. This revealed that Lp(a) might play a role in anti-NTHi infection.
VL  - 3
IS  - 6
ER  -

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Author Information

Liu En

College of Veterinary Science, Inner Mongolia Agriculture University, Hohhot, China
Li Weng-long

College of Veterinary Science, Inner Mongolia Agriculture University, Hohhot, China
Han Run-lin

College of Veterinary Science, Inner Mongolia Agriculture University, Hohhot, China

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APA Style

Liu En, Li Weng-long, Han Run-lin. (2015). The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a). American Journal of Clinical and Experimental Medicine, 3(6), 338-343. https://doi.org/10.11648/j.ajcem.20150306.11

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ACS Style

Liu En; Li Weng-long; Han Run-lin. The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a). Am. J. Clin. Exp. Med. 2015, 3(6), 338-343. doi: 10.11648/j.ajcem.20150306.11

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AMA Style

Liu En, Li Weng-long, Han Run-lin. The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a). Am J Clin Exp Med. 2015;3(6):338-343. doi: 10.11648/j.ajcem.20150306.11

Copy | Download

@article{10.11648/j.ajcem.20150306.11,
  author = {Liu En and Li Weng-long and Han Run-lin},
  title = {The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a)},
  journal = {American Journal of Clinical and Experimental Medicine},
  volume = {3},
  number = {6},
  pages = {338-343},
  doi = {10.11648/j.ajcem.20150306.11},
  url = {https://doi.org/10.11648/j.ajcem.20150306.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajcem.20150306.11},
  abstract = {Protein F (PF) is a surface plasminogen (Plg) receptor on the nontypeable Haemophilus influenza (NTHi). Plg via its lysine binding sites (LBS) can bind to PF. Apolipoprotein(a) [Apo(a)] is one component of Lipoprotein(a) [Lp(a)]. It has Kringle (K) domains, which contain LBS and has a high homology with Plg. Therefore, we speculated that Lp(a) might bind to Plg receptor on the surface of NTHi, subsequently competitively inhibiting the interaction of NTHi with Plg. In this study, recombinant PF (rPF) and its C-terminal lysine residue-deleted variant (rPFΔK) were expressed in E. coli BL21. The interactions of rPF with Plg and Lp(a) were tested by ELISA. The results showed that rPF could bind to Plg and Lp(a). The binding capacity of rPF was significantly higher than that of rPFΔK. The interactions of rPF with Plg and Lp(a) could be inhibited by EACA. 2 mmol/L of EACA significantly inhibited the binding of rPF to Plg, while 0.2 mmol/L of EACA could significantly reduce the binding of rPF to Lp(a). 50 ng/100 μL Lp(a) could significantly inhibit the interaction of rPF with Plg. In addition, affinity chromatography assay followed by Western biotting was also used to study the interaction. In overall, C-terminal lysine residue of rPF and the lysine binding sites (LBS) of Plg and Lp(a) should be responsible for these specifically bindings. Lp(a) could combine with rPF consequently inhibiting the interaction of Plg with rPF. This revealed that Lp(a) might play a role in anti-NTHi infection.},
 year = {2015}
}

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TY  - JOUR
T1  - The Interaction Between Recombinant Protein F Derived from Nontypeable Haemophilus influenza and Lipoprotein(a)
AU  - Liu En
AU  - Li Weng-long
AU  - Han Run-lin
Y1  - 2015/12/05
PY  - 2015
N1  - https://doi.org/10.11648/j.ajcem.20150306.11
DO  - 10.11648/j.ajcem.20150306.11
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  - 338
EP  - 343
PB  - Science Publishing Group
SN  - 2330-8133
UR  - https://doi.org/10.11648/j.ajcem.20150306.11
AB  - Protein F (PF) is a surface plasminogen (Plg) receptor on the nontypeable Haemophilus influenza (NTHi). Plg via its lysine binding sites (LBS) can bind to PF. Apolipoprotein(a) [Apo(a)] is one component of Lipoprotein(a) [Lp(a)]. It has Kringle (K) domains, which contain LBS and has a high homology with Plg. Therefore, we speculated that Lp(a) might bind to Plg receptor on the surface of NTHi, subsequently competitively inhibiting the interaction of NTHi with Plg. In this study, recombinant PF (rPF) and its C-terminal lysine residue-deleted variant (rPFΔK) were expressed in E. coli BL21. The interactions of rPF with Plg and Lp(a) were tested by ELISA. The results showed that rPF could bind to Plg and Lp(a). The binding capacity of rPF was significantly higher than that of rPFΔK. The interactions of rPF with Plg and Lp(a) could be inhibited by EACA. 2 mmol/L of EACA significantly inhibited the binding of rPF to Plg, while 0.2 mmol/L of EACA could significantly reduce the binding of rPF to Lp(a). 50 ng/100 μL Lp(a) could significantly inhibit the interaction of rPF with Plg. In addition, affinity chromatography assay followed by Western biotting was also used to study the interaction. In overall, C-terminal lysine residue of rPF and the lysine binding sites (LBS) of Plg and Lp(a) should be responsible for these specifically bindings. Lp(a) could combine with rPF consequently inhibiting the interaction of Plg with rPF. This revealed that Lp(a) might play a role in anti-NTHi infection.
VL  - 3
IS  - 6
ER  -

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