The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Surface Proteins of Streptococcus agalactiae and Related Proteins in Other Bacterial Pathogens
Open accessAbstract
SUMMARY: Streptococcus agalactiae(group B Streptococcus) is the major cause of invasive bacterial disease, including meningitis, in the neonatal period. Although prophylactic measures have contributed to a substantial reduction in the number of infections, development of a vaccine remains an important goal. While much work in this field has focused on the S. agalactiae polysaccharide capsule, which is an important virulence factor that elicits protective immunity, surface proteins have received increasing attention as potential virulence factors and vaccine components. Here, we summarize current knowledge about S. agalactiae surface proteins, with emphasis on proteins that have been characterized immunochemically and/or elicit protective immunity in animal models. These surface proteins have been implicated in interactions with human epithelial cells, binding to extracellular matrix components, and/or evasion of host immunity. Of note, several S. agalactiae surface proteins are related to surface proteins identified in other bacterial pathogens, emphasizing the general interest of the S. agalactiae proteins. Because some S. agalactiae surface proteins elicit protective immunity, they hold promise as components in a vaccine based only on proteins or as carriers in polysaccharide conjugate vaccines.
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Cites
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“agalactiae pathogenesis, these proteins are of interest as models for other repetitive proteins, which are common in grampositive bacteria (120, 177) and in higher organisms (162, 240, 262).”
Genomic Islands in Pathogenic and Environmental Microorganisms
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A transgenic model for listeriosis: role of internalin in crossing the intestinal barrier
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“In the future, the use of transgenic mice may facilitate studies of some aspects of the infectious process, as described in other systems (100, 143, 207).”
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Sortase, a universal target for therapeutic agents against Gram-positive bacteria?
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Anchorless adhesins and invasins of Gram-positive bacteria: a new class of virulence factors
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Cited by
Streptococcus Adherence and Colonization
Nobbs, A. H., Lamont, R. J., & Jenkinson, H. F. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00014-09 · Cited by 657
Fernandez, A., Lechardeur, D., Derré-Bobillot, A., Couvé, E., Gaudu, P., & Gruss, A. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000860 · Cited by 65
Burcham, L. R., Le Breton, Y., Radin, J. N., Spencer, B. L., Deng, L., Hiron, A., Ransom, M. R., Mendonça, J. D. C., Belew, A. T., El-Sayed, N. M., et al. (2020) · mBio · doi:10.1128/mbio.02302-20 · Cited by 47
Waldemarsson, J., Areschoug, T., Lindahl, G., & Johnsson, E. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.2.378-388.2006 · Cited by 36
Self-citationSpatial Organization of Cell Wall-Anchored Proteins at the Surface of Gram-Positive Bacteria
Dramsi, S., & Bierne, H. (2016) · Current Topics in Microbiology and Immunology · doi:10.1007/82_2016_4 · Cited by 36
Metadata
- Authors
- Lindahl, G., Stålhammar-Carlemalm, M., & Areschoug, T.
- Venue
- Clinical Microbiology Reviews
- Publisher
- American Society for Microbiology
- Published
- 2005-01
- Volume
- 18
- Issue
- 1
- Pages
- 102-127
- ISSN
- 0893-8512 (ISSN-L)
- 1098-6618
- OpenAlex
- W2123958668
- Cited by
- 349
- References
- 7
- FWCI
- 19.41
- Type
- journal article
- Language
- en
- Open access
- green
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- Lindahl, G., Stålhammar-Carlemalm, M., & Areschoug, T. (2005). Surface Proteins of Streptococcus agalactiae and Related Proteins in Other Bacterial Pathogens. Clinical Microbiology Reviews. https://doi.org/10.1128/cmr.18.1.102-127.2005
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.