NlpI contributes to Escherichia coli K1 strain RS218 interaction with human brain microvascular endothelial cells

Ching Hao Teng, Yu Ting Tseng, Ravi Maruvada, Donna Pearce, Yi Xie, Maneesh Paul-Satyaseela, Kwang Sik Kim

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Escherichia coli K1 is the most common Gram-negative bacillary organism causing neonatal meningitis. E. coli K1 binding to and invasion of human brain microvascular endothelial cells (HBMECs) is a prerequisite for its traversal of the blood-brain barrier (BBB) and penetration into the brain. In the present study, we identified NlpI as a novel bacterial determinant contributing to E. coli K1 interaction with HBMECs. The deletion of nlpI did not affect the expression of the known bacterial determinants involved in E. coli K1-HBMEC interaction, such as type 1 fimbriae, flagella, and OmpA, and the contribution of NlpI to HBMECs binding and invasion was independent of those bacterial determinants. Previous reports have shown that the nlpI mutant of E. coli K-12 exhibits growth defect at 42°C at low osmolarity, and its thermosensitive phenotype can be suppressed by a mutation on the spr gene. The nlpI mutant of strain RS218 exhibited similar thermosensitive phenotype, but additional spr mutation did not restore the ability of the nlpI mutant to interact with HBMECs. These findings suggest the decreased ability of the nlpI mutant to interact with HBMECs is not associated with the thermosensitive phenotype. NlpI was determined as an outer membrane-anchored protein in E. coli, and the nlpI mutant was defective in cytosolic phospholipase A2α (cPLA 2α) phosphorylation compared to the parent strain. These findings illustrate the first demonstration of NlpI's contribution to E. coli K1 binding to and invasion of HBMECs, and its contribution is likely to involve cPLA2α.

Original languageEnglish
Pages (from-to)3090-3096
Number of pages7
JournalInfection and Immunity
Volume78
Issue number7
DOIs
Publication statusPublished - 2010 Jul 1

Fingerprint

Endothelial Cells
Escherichia coli
Brain
Phenotype
Cytosolic Phospholipases A2
Mutation
Flagella
Blood-Brain Barrier
Meningitis
Cell Communication
Osmolar Concentration
Membrane Proteins
Phosphorylation
Growth
Genes

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

Cite this

Teng, Ching Hao ; Tseng, Yu Ting ; Maruvada, Ravi ; Pearce, Donna ; Xie, Yi ; Paul-Satyaseela, Maneesh ; Kim, Kwang Sik. / NlpI contributes to Escherichia coli K1 strain RS218 interaction with human brain microvascular endothelial cells. In: Infection and Immunity. 2010 ; Vol. 78, No. 7. pp. 3090-3096.
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NlpI contributes to Escherichia coli K1 strain RS218 interaction with human brain microvascular endothelial cells. / Teng, Ching Hao; Tseng, Yu Ting; Maruvada, Ravi; Pearce, Donna; Xie, Yi; Paul-Satyaseela, Maneesh; Kim, Kwang Sik.

In: Infection and Immunity, Vol. 78, No. 7, 01.07.2010, p. 3090-3096.

Research output: Contribution to journalArticle

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AU - Teng, Ching Hao

AU - Tseng, Yu Ting

AU - Maruvada, Ravi

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AU - Xie, Yi

AU - Paul-Satyaseela, Maneesh

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N2 - Escherichia coli K1 is the most common Gram-negative bacillary organism causing neonatal meningitis. E. coli K1 binding to and invasion of human brain microvascular endothelial cells (HBMECs) is a prerequisite for its traversal of the blood-brain barrier (BBB) and penetration into the brain. In the present study, we identified NlpI as a novel bacterial determinant contributing to E. coli K1 interaction with HBMECs. The deletion of nlpI did not affect the expression of the known bacterial determinants involved in E. coli K1-HBMEC interaction, such as type 1 fimbriae, flagella, and OmpA, and the contribution of NlpI to HBMECs binding and invasion was independent of those bacterial determinants. Previous reports have shown that the nlpI mutant of E. coli K-12 exhibits growth defect at 42°C at low osmolarity, and its thermosensitive phenotype can be suppressed by a mutation on the spr gene. The nlpI mutant of strain RS218 exhibited similar thermosensitive phenotype, but additional spr mutation did not restore the ability of the nlpI mutant to interact with HBMECs. These findings suggest the decreased ability of the nlpI mutant to interact with HBMECs is not associated with the thermosensitive phenotype. NlpI was determined as an outer membrane-anchored protein in E. coli, and the nlpI mutant was defective in cytosolic phospholipase A2α (cPLA 2α) phosphorylation compared to the parent strain. These findings illustrate the first demonstration of NlpI's contribution to E. coli K1 binding to and invasion of HBMECs, and its contribution is likely to involve cPLA2α.

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