Evidence map›Paper›PMID 10449784›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

A 21-kDa surface protein of Mycobacterium leprae binds peripheral nerve laminin-2 and mediates Schwann cell invasion.

Y Shimoji, V Ng, K Matsumura, V A Fischetti, A Rambukkana

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
5.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

49 citing papers in PubMed, 140 citations in OpenAlex.

  1. Article
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  7. Iron uptake and transport by the carboxymycobactin-mycobactin siderophore machinery of Mycobacterium tuberculosis is dependent on the iron-regulated protein HupB.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021
    Article
  8. TLR-9 Plays a Role inFrontiers in immunology · 2021
    Article
  9. Review
  10. Article
  11. Article
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  16. Laminin targeting of a peripheral nerve-highlighting peptide enables degenerated nerve visualization.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Y ShimojiLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10021, USA.
V Ng
K Matsumura
V A Fischetti
A Rambukkana
Teikyo University · JPRockefeller University · US

Funding

MYCOBACTERIUM LEPRAE ANTIGENS AND NERVE DAMAGER01AI045816 · NIAID · ROCKEFELLER UNIVERSITY · PI RAMBUKKANA, ANURA · 1999 to 2009
$2.6M
NIAID NIH HHS AI45816NIAID NIH HHS R01 AI045816
6 · The paper itself

Abstract

Nerve damage is the hallmark of Mycobacterium leprae infection, which results from M. leprae invasion of the Schwann cell of the peripheral nervous system. We have recently shown that the laminin-2 isoform, specially the G domain of laminin alpha2 chain, on the Schwann cell-axon unit serves as an initial neural target for M. leprae. However, M. leprae surface molecules that mediate bacterial invasion of peripheral nerves are entirely unknown. By using human alpha2 laminins as a probe, a major 28-kDa protein in the M. leprae cell wall fraction that binds alpha2 laminins was identified. After N-terminal amino acid sequence analysis, PCR-based strategy was used to clone the gene that encodes this protein. Deduced amino acid sequence of this M. leprae laminin-binding protein predicts a 21-kDa molecule (ML-LBP21), which is smaller than the observed molecular size in SDS/PAGE. Immunofluorescence and immunoelectron microscopy on intact M. leprae with mAbs against recombinant (r) ML-LBP21 revealed that the protein is surface exposed. rML-LBP21 avidly bound to alpha2 laminins, the rG domain of the laminin-alpha2 chain, and the native peripheral nerve laminin-2. The role of ML-LBP21 in Schwann cell adhesion and invasion was investigated by using fluorescent polystyrene beads coated with rML-LBP21. Although beads coated with rML-LBP21 alone specifically adhered to and were ingested by primary Schwann cells, these functions were significantly enhanced when beads were preincubated with exogenous alpha2 laminins. Taken together, the present data suggest that ML-LBP21 may function as a critical surface adhesin that facilitates the entry of M. leprae into Schwann cells.

Indexed as

Adhesins, BacterialAmino Acid SequenceAnimalsBase SequenceCells, CulturedCell WallElectrophoresis, Polyacrylamide GelHumansLamininLeprosyMiceMice, Inbred BALB CMicroscopy, ImmunoelectronMolecular Sequence DataMolecular WeightMycobacterium lepraeAdhesins, BacterialLamininlaminin alpha 2ML-LBP21

Identifiers

PMID10449784
PMCPMC22300
OpenAlexW2008301887

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.