Interaction of human mannose-binding protein with Mycobacterium avium

Vsevolod Y. Polotsky, John T. Belisle, Katarina Mikusova, R. Alan B Ezekowitz, Keith A Joiner

Research output: Contribution to journalArticle

70 Citations (Scopus)

Abstract

The interaction between human mannose-binding protein (MBP) and Mycobacterium avium was explored. By ELISA, calcium-dependent and mannan- inhibitable binding of human recombinant MBP (rMBP) to live M. avium was observed. Preincubation of M. avium with rMBP resulted in a 2-fold increase in uptake by human neutrophils. Mycobacterial cell wall components were assessed by ELISA for their ability to bind the carbohydrate recognition domain of rMBP. The best ligand was mannosyl-lipoarabinomannan, followed by lipomannan, phosphatidylinositol mannoside, arabinosyl-lipoarabinomannan, and dimycolated trehalose (cord factor). rMBP did not bind to partially purified lipid fractions containing glycopeptidolipids. These results are consistent with the known structural basis for rMBP ligand recognition. They suggest that MBP may play a role in host defense against M. avium by opsonizing both whole organisms and free cell wall components for internalization.

Original languageEnglish (US)
Pages (from-to)1159-1168
Number of pages10
JournalJournal of Infectious Diseases
Volume175
Issue number5
StatePublished - 1997
Externally publishedYes

Fingerprint

Mannose-Binding Lectin
Mycobacterium avium
Cellular Structures
Cell Wall
Cord Factors
Enzyme-Linked Immunosorbent Assay
Ligands
Mannans
Trehalose
Recombinant Proteins
Neutrophils
Carbohydrates
Calcium
Lipids
lipoarabinomannan

ASJC Scopus subject areas

  • Public Health, Environmental and Occupational Health
  • Immunology

Cite this

Polotsky, V. Y., Belisle, J. T., Mikusova, K., Ezekowitz, R. A. B., & Joiner, K. A. (1997). Interaction of human mannose-binding protein with Mycobacterium avium. Journal of Infectious Diseases, 175(5), 1159-1168.

Interaction of human mannose-binding protein with Mycobacterium avium. / Polotsky, Vsevolod Y.; Belisle, John T.; Mikusova, Katarina; Ezekowitz, R. Alan B; Joiner, Keith A.

In: Journal of Infectious Diseases, Vol. 175, No. 5, 1997, p. 1159-1168.

Research output: Contribution to journalArticle

Polotsky, VY, Belisle, JT, Mikusova, K, Ezekowitz, RAB & Joiner, KA 1997, 'Interaction of human mannose-binding protein with Mycobacterium avium', Journal of Infectious Diseases, vol. 175, no. 5, pp. 1159-1168.
Polotsky VY, Belisle JT, Mikusova K, Ezekowitz RAB, Joiner KA. Interaction of human mannose-binding protein with Mycobacterium avium. Journal of Infectious Diseases. 1997;175(5):1159-1168.
Polotsky, Vsevolod Y. ; Belisle, John T. ; Mikusova, Katarina ; Ezekowitz, R. Alan B ; Joiner, Keith A. / Interaction of human mannose-binding protein with Mycobacterium avium. In: Journal of Infectious Diseases. 1997 ; Vol. 175, No. 5. pp. 1159-1168.
@article{7e4019a9685b44fe8616f74c0d5d8980,
title = "Interaction of human mannose-binding protein with Mycobacterium avium",
abstract = "The interaction between human mannose-binding protein (MBP) and Mycobacterium avium was explored. By ELISA, calcium-dependent and mannan- inhibitable binding of human recombinant MBP (rMBP) to live M. avium was observed. Preincubation of M. avium with rMBP resulted in a 2-fold increase in uptake by human neutrophils. Mycobacterial cell wall components were assessed by ELISA for their ability to bind the carbohydrate recognition domain of rMBP. The best ligand was mannosyl-lipoarabinomannan, followed by lipomannan, phosphatidylinositol mannoside, arabinosyl-lipoarabinomannan, and dimycolated trehalose (cord factor). rMBP did not bind to partially purified lipid fractions containing glycopeptidolipids. These results are consistent with the known structural basis for rMBP ligand recognition. They suggest that MBP may play a role in host defense against M. avium by opsonizing both whole organisms and free cell wall components for internalization.",
author = "Polotsky, {Vsevolod Y.} and Belisle, {John T.} and Katarina Mikusova and Ezekowitz, {R. Alan B} and Joiner, {Keith A}",
year = "1997",
language = "English (US)",
volume = "175",
pages = "1159--1168",
journal = "Journal of Infectious Diseases",
issn = "0022-1899",
publisher = "Oxford University Press",
number = "5",

}

TY - JOUR

T1 - Interaction of human mannose-binding protein with Mycobacterium avium

AU - Polotsky, Vsevolod Y.

AU - Belisle, John T.

AU - Mikusova, Katarina

AU - Ezekowitz, R. Alan B

AU - Joiner, Keith A

PY - 1997

Y1 - 1997

N2 - The interaction between human mannose-binding protein (MBP) and Mycobacterium avium was explored. By ELISA, calcium-dependent and mannan- inhibitable binding of human recombinant MBP (rMBP) to live M. avium was observed. Preincubation of M. avium with rMBP resulted in a 2-fold increase in uptake by human neutrophils. Mycobacterial cell wall components were assessed by ELISA for their ability to bind the carbohydrate recognition domain of rMBP. The best ligand was mannosyl-lipoarabinomannan, followed by lipomannan, phosphatidylinositol mannoside, arabinosyl-lipoarabinomannan, and dimycolated trehalose (cord factor). rMBP did not bind to partially purified lipid fractions containing glycopeptidolipids. These results are consistent with the known structural basis for rMBP ligand recognition. They suggest that MBP may play a role in host defense against M. avium by opsonizing both whole organisms and free cell wall components for internalization.

AB - The interaction between human mannose-binding protein (MBP) and Mycobacterium avium was explored. By ELISA, calcium-dependent and mannan- inhibitable binding of human recombinant MBP (rMBP) to live M. avium was observed. Preincubation of M. avium with rMBP resulted in a 2-fold increase in uptake by human neutrophils. Mycobacterial cell wall components were assessed by ELISA for their ability to bind the carbohydrate recognition domain of rMBP. The best ligand was mannosyl-lipoarabinomannan, followed by lipomannan, phosphatidylinositol mannoside, arabinosyl-lipoarabinomannan, and dimycolated trehalose (cord factor). rMBP did not bind to partially purified lipid fractions containing glycopeptidolipids. These results are consistent with the known structural basis for rMBP ligand recognition. They suggest that MBP may play a role in host defense against M. avium by opsonizing both whole organisms and free cell wall components for internalization.

UR - http://www.scopus.com/inward/record.url?scp=0030911989&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030911989&partnerID=8YFLogxK

M3 - Article

C2 - 9129080

AN - SCOPUS:0030911989

VL - 175

SP - 1159

EP - 1168

JO - Journal of Infectious Diseases

JF - Journal of Infectious Diseases

SN - 0022-1899

IS - 5

ER -