Escherichia coli Braun Lipoprotein (BLP) exhibits endotoxemia - Like pathology in Swiss albino mice

Chikkamenahalli Lakshminarayana Lakshmikanth, Shancy Petsel Jacob, Avinash Kundadka Kudva, Calivarathan Latchoumycandane, Puttaraju Srikanta Murthy Yashaswini, Mosale Seetharam Sumanth, Cassiano F. Goncalves-De-Albuquerque, Adriana R. Silva, Sridevi Annapurna Singh, Hugo C. Castro-Faria-Neto, Sandeep Kumble Prabhu, Thomas M. McIntyre, Gopal Kedihithlu Marathe

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Abstract

The endotoxin lipopolysaccharide (LPS) promotes sepsis, but bacterial peptides also promote inflammation leading to sepsis. We found, intraperitoneal administration of live or heat inactivated E. coli JE5505 lacking the abundant outer membrane protein, Braun lipoprotein (BLP), was less toxic than E. coli DH5α possessing BLP in Swiss albino mice. Injection of BLP free of LPS purified from E. coli DH5α induced massive infiltration of leukocytes in lungs and liver. BLP activated human polymorphonuclear cells (PMNs) ex vivo to adhere to denatured collagen in serum and polymyxin B independent fashion, a property distinct from LPS. Both LPS and BLP stimulated the synthesis of platelet activating factor (PAF), a potent lipid mediator, in human PMNs. In mouse macrophage cell line, RAW264.7, while both BLP and LPS similarly upregulated TNF-α and IL-1β mRNA; BLP was more potent in inducing cyclooxygenase-2 (COX-2) mRNA and protein expression. Peritoneal macrophages from TLR2 -/- mice significantly reduced the production of TNF-α in response to BLP in contrast to macrophages from wild type mice. We conclude, BLP acting through TLR2, is a potent inducer of inflammation with a response profile both common and distinct from LPS. Hence, BLP mediated pathway may also be considered as an effective target against sepsis.

Original languageEnglish (US)
Article number34666
JournalScientific reports
Volume6
DOIs
StatePublished - Oct 4 2016

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Endotoxemia
Lipoproteins
Pathology
Escherichia coli
Lipopolysaccharides
Sepsis
Macrophages
Inflammation
Polymyxin B
Messenger RNA
Poisons
Platelet Activating Factor
Peritoneal Macrophages
Cyclooxygenase 2
Interleukin-1
Endotoxins
Membrane Proteins
Leukocytes
Collagen
Hot Temperature

All Science Journal Classification (ASJC) codes

  • General

Cite this

Lakshmikanth, C. L., Jacob, S. P., Kudva, A. K., Latchoumycandane, C., Yashaswini, P. S. M., Sumanth, M. S., ... Marathe, G. K. (2016). Escherichia coli Braun Lipoprotein (BLP) exhibits endotoxemia - Like pathology in Swiss albino mice. Scientific reports, 6, [34666]. https://doi.org/10.1038/srep34666
Lakshmikanth, Chikkamenahalli Lakshminarayana ; Jacob, Shancy Petsel ; Kudva, Avinash Kundadka ; Latchoumycandane, Calivarathan ; Yashaswini, Puttaraju Srikanta Murthy ; Sumanth, Mosale Seetharam ; Goncalves-De-Albuquerque, Cassiano F. ; Silva, Adriana R. ; Singh, Sridevi Annapurna ; Castro-Faria-Neto, Hugo C. ; Prabhu, Sandeep Kumble ; McIntyre, Thomas M. ; Marathe, Gopal Kedihithlu. / Escherichia coli Braun Lipoprotein (BLP) exhibits endotoxemia - Like pathology in Swiss albino mice. In: Scientific reports. 2016 ; Vol. 6.
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title = "Escherichia coli Braun Lipoprotein (BLP) exhibits endotoxemia - Like pathology in Swiss albino mice",
abstract = "The endotoxin lipopolysaccharide (LPS) promotes sepsis, but bacterial peptides also promote inflammation leading to sepsis. We found, intraperitoneal administration of live or heat inactivated E. coli JE5505 lacking the abundant outer membrane protein, Braun lipoprotein (BLP), was less toxic than E. coli DH5α possessing BLP in Swiss albino mice. Injection of BLP free of LPS purified from E. coli DH5α induced massive infiltration of leukocytes in lungs and liver. BLP activated human polymorphonuclear cells (PMNs) ex vivo to adhere to denatured collagen in serum and polymyxin B independent fashion, a property distinct from LPS. Both LPS and BLP stimulated the synthesis of platelet activating factor (PAF), a potent lipid mediator, in human PMNs. In mouse macrophage cell line, RAW264.7, while both BLP and LPS similarly upregulated TNF-α and IL-1β mRNA; BLP was more potent in inducing cyclooxygenase-2 (COX-2) mRNA and protein expression. Peritoneal macrophages from TLR2 -/- mice significantly reduced the production of TNF-α in response to BLP in contrast to macrophages from wild type mice. We conclude, BLP acting through TLR2, is a potent inducer of inflammation with a response profile both common and distinct from LPS. Hence, BLP mediated pathway may also be considered as an effective target against sepsis.",
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Lakshmikanth, CL, Jacob, SP, Kudva, AK, Latchoumycandane, C, Yashaswini, PSM, Sumanth, MS, Goncalves-De-Albuquerque, CF, Silva, AR, Singh, SA, Castro-Faria-Neto, HC, Prabhu, SK, McIntyre, TM & Marathe, GK 2016, 'Escherichia coli Braun Lipoprotein (BLP) exhibits endotoxemia - Like pathology in Swiss albino mice', Scientific reports, vol. 6, 34666. https://doi.org/10.1038/srep34666

Escherichia coli Braun Lipoprotein (BLP) exhibits endotoxemia - Like pathology in Swiss albino mice. / Lakshmikanth, Chikkamenahalli Lakshminarayana; Jacob, Shancy Petsel; Kudva, Avinash Kundadka; Latchoumycandane, Calivarathan; Yashaswini, Puttaraju Srikanta Murthy; Sumanth, Mosale Seetharam; Goncalves-De-Albuquerque, Cassiano F.; Silva, Adriana R.; Singh, Sridevi Annapurna; Castro-Faria-Neto, Hugo C.; Prabhu, Sandeep Kumble; McIntyre, Thomas M.; Marathe, Gopal Kedihithlu.

In: Scientific reports, Vol. 6, 34666, 04.10.2016.

Research output: Contribution to journalArticle

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AU - Lakshmikanth, Chikkamenahalli Lakshminarayana

AU - Jacob, Shancy Petsel

AU - Kudva, Avinash Kundadka

AU - Latchoumycandane, Calivarathan

AU - Yashaswini, Puttaraju Srikanta Murthy

AU - Sumanth, Mosale Seetharam

AU - Goncalves-De-Albuquerque, Cassiano F.

AU - Silva, Adriana R.

AU - Singh, Sridevi Annapurna

AU - Castro-Faria-Neto, Hugo C.

AU - Prabhu, Sandeep Kumble

AU - McIntyre, Thomas M.

AU - Marathe, Gopal Kedihithlu

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N2 - The endotoxin lipopolysaccharide (LPS) promotes sepsis, but bacterial peptides also promote inflammation leading to sepsis. We found, intraperitoneal administration of live or heat inactivated E. coli JE5505 lacking the abundant outer membrane protein, Braun lipoprotein (BLP), was less toxic than E. coli DH5α possessing BLP in Swiss albino mice. Injection of BLP free of LPS purified from E. coli DH5α induced massive infiltration of leukocytes in lungs and liver. BLP activated human polymorphonuclear cells (PMNs) ex vivo to adhere to denatured collagen in serum and polymyxin B independent fashion, a property distinct from LPS. Both LPS and BLP stimulated the synthesis of platelet activating factor (PAF), a potent lipid mediator, in human PMNs. In mouse macrophage cell line, RAW264.7, while both BLP and LPS similarly upregulated TNF-α and IL-1β mRNA; BLP was more potent in inducing cyclooxygenase-2 (COX-2) mRNA and protein expression. Peritoneal macrophages from TLR2 -/- mice significantly reduced the production of TNF-α in response to BLP in contrast to macrophages from wild type mice. We conclude, BLP acting through TLR2, is a potent inducer of inflammation with a response profile both common and distinct from LPS. Hence, BLP mediated pathway may also be considered as an effective target against sepsis.

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Lakshmikanth CL, Jacob SP, Kudva AK, Latchoumycandane C, Yashaswini PSM, Sumanth MS et al. Escherichia coli Braun Lipoprotein (BLP) exhibits endotoxemia - Like pathology in Swiss albino mice. Scientific reports. 2016 Oct 4;6. 34666. https://doi.org/10.1038/srep34666