Surfactant Protein A (SP-A) Mediates Attachment of Mycobacterium tuberculosis to Murine Alveolar Macrophages

Rajamouli Pasula, James F. Downing, Jo Rae Wright, Diane L. Kachel, Thomas Davis, William J. Martin

Research output: Contribution to journalArticle

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Abstract

Attachment of Mycobacterium tuberculosis organisms to alveolar macrophages (AMs) is an essential early event in primary pulmonary tuberculosis. Surfactant protein A (SP-A) is a nonimmune opsonin present in the alveolar spaces that binds carbohydrate residues such as mannose. It was hypothesized that SP-A attaches to M. tuberculosis and serves as a ligand between M. tuberculosis and AMs. [125I]SP-A was found to bind to M. tuberculosis in a time- and [Ca2+]-dependent manner with a Kd of 1.9 × 10-9 M and an apparent number of 6.3 × 102 SP-A binding sites/organism. Further, deglycosylated SP-A had minimal binding to M. tuberculosis, indicating that sugar moieties are important in this interaction. SP-A specifically binds to a 60-kD cell-wall protein from M. tuberculosis. SP-A-mediated attachment of 51Cr-labeled M. tuberculosis organisms to AMs is dependent on time, SP-A concentration, and Ca2+. M. tuberculosis attachment to murine AMs in the absence of SP-A was 12.8 ± 0.9%; however, in the presence of 5 μg/ml SP-A the attachment increased to 38.6 ± 2.9% (P <0.001). SP-A-mediated attachment was significantly decreased from 38.6 ± 2.9% to 18.7 ± 3.3% (P <0.05) in the presence of antihuman SP-A antibodies. When the attachment assay was repeated in the presence of α-methylene-D-mannosepyranosidase (mannosyl-BSA) and type V collagen, SP-A-mediated attachment decreased from 38.6 ± 2.9% to 16.6 ± 1.5% (P <0.001) and 19.1 ± 1.4% (P <0.05), respectively. Further, deglycosylated SP-A had only a minimal effect on M. tuberculosis attachment to AMs. These data indicate that SP-A can mediate M. tuberculosis attachment to AMs, and suggest possible underlying mechanisms for this.

Original languageEnglish (US)
Pages (from-to)209-217
Number of pages9
JournalAmerican Journal of Respiratory Cell and Molecular Biology
Volume17
Issue number2
StatePublished - 1997
Externally publishedYes

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Pulmonary Surfactant-Associated Protein A
Alveolar Macrophages
Mycobacterium tuberculosis
Collagen Type V
Opsonin Proteins
Mannose

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Pulmonary and Respiratory Medicine

Cite this

Surfactant Protein A (SP-A) Mediates Attachment of Mycobacterium tuberculosis to Murine Alveolar Macrophages. / Pasula, Rajamouli; Downing, James F.; Wright, Jo Rae; Kachel, Diane L.; Davis, Thomas; Martin, William J.

In: American Journal of Respiratory Cell and Molecular Biology, Vol. 17, No. 2, 1997, p. 209-217.

Research output: Contribution to journalArticle

Pasula, Rajamouli ; Downing, James F. ; Wright, Jo Rae ; Kachel, Diane L. ; Davis, Thomas ; Martin, William J. / Surfactant Protein A (SP-A) Mediates Attachment of Mycobacterium tuberculosis to Murine Alveolar Macrophages. In: American Journal of Respiratory Cell and Molecular Biology. 1997 ; Vol. 17, No. 2. pp. 209-217.
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abstract = "Attachment of Mycobacterium tuberculosis organisms to alveolar macrophages (AMs) is an essential early event in primary pulmonary tuberculosis. Surfactant protein A (SP-A) is a nonimmune opsonin present in the alveolar spaces that binds carbohydrate residues such as mannose. It was hypothesized that SP-A attaches to M. tuberculosis and serves as a ligand between M. tuberculosis and AMs. [125I]SP-A was found to bind to M. tuberculosis in a time- and [Ca2+]-dependent manner with a Kd of 1.9 × 10-9 M and an apparent number of 6.3 × 102 SP-A binding sites/organism. Further, deglycosylated SP-A had minimal binding to M. tuberculosis, indicating that sugar moieties are important in this interaction. SP-A specifically binds to a 60-kD cell-wall protein from M. tuberculosis. SP-A-mediated attachment of 51Cr-labeled M. tuberculosis organisms to AMs is dependent on time, SP-A concentration, and Ca2+. M. tuberculosis attachment to murine AMs in the absence of SP-A was 12.8 ± 0.9{\%}; however, in the presence of 5 μg/ml SP-A the attachment increased to 38.6 ± 2.9{\%} (P <0.001). SP-A-mediated attachment was significantly decreased from 38.6 ± 2.9{\%} to 18.7 ± 3.3{\%} (P <0.05) in the presence of antihuman SP-A antibodies. When the attachment assay was repeated in the presence of α-methylene-D-mannosepyranosidase (mannosyl-BSA) and type V collagen, SP-A-mediated attachment decreased from 38.6 ± 2.9{\%} to 16.6 ± 1.5{\%} (P <0.001) and 19.1 ± 1.4{\%} (P <0.05), respectively. Further, deglycosylated SP-A had only a minimal effect on M. tuberculosis attachment to AMs. These data indicate that SP-A can mediate M. tuberculosis attachment to AMs, and suggest possible underlying mechanisms for this.",
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T1 - Surfactant Protein A (SP-A) Mediates Attachment of Mycobacterium tuberculosis to Murine Alveolar Macrophages

AU - Pasula, Rajamouli

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AU - Davis, Thomas

AU - Martin, William J.

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