Evidence map›Paper›PMID 9712778›Full record

ArticleInfection and immunity1998

Deletion of the central proline-rich repeat domain results in altered antigenicity and lack of surface expression of the Streptococcus mutans P1 adhesin molecule.

L J Brady, D G Cvitkovitch, C M Geric, M N Addison, J C Joyce, P J Crowley, A S Bleiweis

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. The Combinations Chitosan-PamInfection and immunity · 2019
    Article
  3. Article
  4. Article
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  6. An intramolecular lock facilitates folding and stabilizes the tertiary structure of Streptococcus mutans adhesin P1.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  7. Article
  8. Article
  9. Article
  10. Functional amyloid formation by Streptococcus mutans.Microbiology (Reading, England) · 2012
    Article
  11. Article
  12. Article
  13. Article
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  15. Article
  16. Review
  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

7 authors at 1 institution in 1 country.

L J BradyDepartment of Oral Biology, University of Florida, Gainesville, Florida 32610, USA. jbrady@dental.ufl.edu
D G Cvitkovitch
C M Geric
M N Addison
J C Joyce
P J Crowley
A S Bleiweis
University of Florida · US

Funding

MEMBRANES OF THE DENTAL PATHOGEN STREPTOCOCCUS MUTANSR01DE008007 · NIDCR · UNIVERSITY OF FLORIDA · PI L. Jeannine Brady, Surabhi Mishra · 1986 to 2026
$8.6M
MEMBRANES OF THE DENTAL PATHOGEN STREPTOCOCCUS MUTANSR37DE008007 · NIDCR · UNIVERSITY OF FLORIDA · PI BLEIWEIS, ARNOLD S. · 1988 to 1997
–
NIDCR NIH HHS DE08007-12NIDCR NIH HHS R01 DE008007
6 · The paper itself

Abstract

Members of the family of surface adhesins of oral streptococci, including P1 of Streptococcus mutans, contain two highly conserved repeat domains, one rich in alanine (A region) and the other rich in proline (P region). To assess the contribution of the P region to the biological properties of P1, an internal deletion in spaP was engineered. In addition, the P region was subcloned and expressed as a fusion partner with the maltose binding protein of Escherichia coli and liberated by digestion with factor Xa. Results of Western blot experiments in which recombinant polypeptides were probed with a panel of 11 monoclonal antibodies indicated that the P region is a necessary component of conformational epitopes within the central portion of P1. Antibodies reactive with the P region were detected in a polyclonal rabbit antiserum generated against whole S. mutans cells but not in two rabbit antisera generated against purified P1 (Mr approximately 185,000), suggesting that this domain is immunogenic on the surface of intact bacteria but not as part of a soluble full-length molecule. Finally, transformation of a spaP-negative mutant with a shuttle vector containing an internally deleted spaP lacking P-region DNA resulted in a complete absence of surface-localized P1 and substantially less P1 in sonicated cells compared to the case for the mutant complemented with the full-length gene. These results suggest that the P region is an integral component contributing to the conformation of the central region of P1 and indicate that its presence is necessary for surface expression of the molecule on S. mutans.

Indexed as

Membrane GlycoproteinsRepetitive Sequences, Nucleic AcidAdhesins, BacterialAnimalsAntibodies, MonoclonalAntigens, BacterialBacterial ProteinsBlotting, WesternEpitopes, B-LymphocyteEscherichia coliMicePlasmidsProlineRabbitsRNA, MessengerSequence DeletionAdhesins, BacterialAntibodies, MonoclonalAntigens, BacterialBacterial ProteinsEpitopes, B-LymphocyteMembrane GlycoproteinsProlineRNA, MessengerS-layer proteins

Identifiers

PMID9712778
PMCPMC108516
OpenAlexW2120636265

What OpenQuestion holds

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Registered trials

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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.