The Group B Streptococcal surface antigen I/II protein, BspC, interacts with host vimentin to promote adherence to brain endothelium and inflammation during the pathogenesis of meningitis.

Deng, Liwen; Spencer, Brady L.; Holmes, Joshua A.; Mu, Rong; Rego, Sara; Weston, Thomas A.; Hu, Yoonsung; Sanches, Glenda F.; Yoon, Sunghyun; Park, Nogi; Nagao, Prescilla E.; Jenkinson, Howard F.; Thornton, Justin A.; Seo, Keun Seok; Nobbs, Angela H.; Doran, Kelly S.

doi:10.1371/journal.ppat.1007848

Cited by 74Neonatal and Maternal InfectionsBacterial Infections and VaccinesStreptococcal Infections and Treatments

The Group B Streptococcal surface antigen I/II protein, BspC, interacts with host vimentin to promote adherence to brain endothelium and inflammation during the pathogenesis of meningitis.

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Deng, Liwen, Spencer, Brady L., Holmes, Joshua A., Mu, Rong, Rego, Sara, Weston, Thomas A., Hu, Yoonsung, Sanches, Glenda F. +8 more·2019·PLOS Pathogens

DOI 10.1371/journal.ppat.1007848PMC PMC6586375

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Abstract

Streptococcus agalactiae (Group B Streptococcus, GBS) normally colonizes healthy adults but can cause invasive disease, such as meningitis, in the newborn. To gain access to the central nervous system, GBS must interact with and penetrate brain or meningeal blood vessels; however, the exact mechanisms are still being elucidated. Here, we investigate the contribution of BspC, an antigen I/II family adhesin, to the pathogenesis of GBS meningitis. Disruption of the bspC gene reduced GBS adherence to human cerebral microvascular endothelial cells (hCMEC), while heterologous expression of BspC in non-adherent Lactococcus lactis conferred bacterial attachment. In a murine model of hematogenous meningitis, mice infected with ΔbspC mutants exhibited lower mortality as well as decreased brain bacterial counts and inflammatory infiltrate compared to mice infected with WT GBS strains. Further, BspC was both necessary and sufficient to induce neutrophil chemokine expression. We determined that BspC interacts with the host cytoskeleton component vimentin and confirmed this interaction using a bacterial two-hybrid assay, microscale thermophoresis, immunofluorescent staining, and imaging flow cytometry. Vimentin null mice were protected from WT GBS infection and also exhibited less inflammatory cytokine production in brain tissue. These results suggest that BspC and the vimentin interaction is critical for the pathogenesis of GBS meningitis.

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All major meningitis causing bacteria can adhere strongly to meningeal fibroblasts and arachnoid barrier-like cells, and Group B Streptococcus bacteria cross the blood brain barrier by binding to vimentin on endothelial cells, which is also highly expressed by arachnoid barrier cells.
“All major meningitis causing bacteria can adhere strongly to meningeal fibroblasts and arachnoid barrier-like cells”
From Living on the Edge of the CNS: Meninges Cell Diversity in Health and Disease (2021) · cites this paper as Deng et al., 2019

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Meningitic Escherichia coli Induction of ANGPTL4 in Brain Microvascular Endothelial Cells Contributes to Blood–Brain Barrier Disruption via ARHGAP5/RhoA/MYL5 Signaling Cascade
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Community-acquired bacterial meningitis.
van de Beek, D., Brouwer, M. C., Koedel, U., & Wall, E. C. (2021) · The Lancet · doi:10.1016/s0140-6736(21)00883-7 · Cited by 292 · see citing works
Bacteria hijack a meningeal neuroimmune axis to facilitate brain invasion
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Vimentin: Regulation and pathogenesis
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Group B Streptococcal Neonatal Meningitis
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Mechanical and Non‐Mechanical Functions of Filamentous and Non‐Filamentous Vimentin
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Vimentin as a potential target for diverse nervous system diseases
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Virulence Factors of Meningitis-Causing Bacteria: Enabling Brain Entry across the Blood–Brain Barrier
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Identification of Zinc-Dependent Mechanisms Used by Group B <i>Streptococcus</i> To Overcome Calprotectin-Mediated Stress
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 · see citing works
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Group B Streptococcus adaptation promotes survival in a hyperinflammatory diabetic wound environment
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A current review of pathogenicity determinants of Streptococcus sp.
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SssP1, a Fimbria-like component of Streptococcus suis, binds to the vimentin of host cells and contributes to bacterial meningitis
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Manzer, H. S., Nobbs, A. H., & Doran, K. S. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.602305 · Cited by 35 · see citing works
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Bacterial protein domains with a novel Ig‐like fold target human CEACAM receptors
van Sorge, N. M., Bonsor, D. A., Deng, L., Lindahl, E. R., Schmitt, V., Lyndіn, M., Schmidt, A., Nilsson, O. R., Brizuela, J., Boero, E., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020106103 · Cited by 34 · see citing works
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Bacterial and Host Determinants of Group B Streptococcal Infection of the Neonate and Infant
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Studying molecular interactions via capillary electrophoresis and microscale thermophoresis: A review
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The Coxiella burnetii T4SS Effector AnkF Is Important for Intracellular Replication
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Dynamic monitoring of CD45-/CD31+/DAPI+ circulating endothelial cells aneuploid for chromosome 8 during neoadjuvant chemotherapy in locally advanced breast cancer
Ma, G., Jiang, Y., Liang, M., Li, J., Wang, J., Mao, X., Veeramootoo, J. S., Xia, T., Liu, X., & Wang, S. (2020) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758835920918470 · Cited by 26 · see citing works
Meningitic Escherichia coli Induction of ANGPTL4 in Brain Microvascular Endothelial Cells Contributes to Blood–Brain Barrier Disruption via ARHGAP5/RhoA/MYL5 Signaling Cascade
Liu, L., Li, J., Huo, D., Peng, Z., Yang, R., Fu, J., Xu, B., Yang, B., Chen, H., & Wang, X. (2019) · Pathogens · doi:10.3390/pathogens8040254 · Cited by 24 · see citing works
Streptococcal autolysin promotes dysfunction of swine tracheal epithelium by interacting with vimentin
Meng, Y., Wáng, Q., Ma, Z., Li, W., Niu, K., Zhu, T., Lin, H., Lu, C., & Fan, H. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010765 · Cited by 21 · see citing works
Membrane vesicle delivery of a streptococcal M protein disrupts the blood–brain barrier by inducing autophagic endothelial cell death
Pan, F., Zhu, M., Liang, Y., Yuan, C., Zhang, Y., Wang, Y.-C., Fan, H., Waldor, M. K., & Ma, Z. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2219435120 · Cited by 21 · see citing works
Vimentin affects inflammation and neutrophil recruitment in airway epithelium during Streptococcus suis serotype 2 infection
Meng, Y., Lin, S., Niu, K., Ma, Z., Lin, H., & Fan, H. (2023) · Veterinary Research · doi:10.1186/s13567-023-01135-3 · Cited by 19 · see citing works
Genome-Wide Screens Identify Group A Streptococcus Surface Proteins Promoting Female Genital Tract Colonization and Virulence
Zhu, L., Olsen, R. J., Beres, S. B., Saavedra, M. O., Kubiak, S. L., Cantu, C. C., Jenkins, L., Yerramilli, P., Pruitt, L., Charbonneau, A. R. L., et al. (2020) · American Journal Of Pathology · doi:10.1016/j.ajpath.2019.12.003 · Cited by 18 · see citing works
Streptococcus agalactiae glycolipids promote virulence by thwarting immune cell clearance
Joyce, L. R., Kim, S., Spencer, B. L., Christensen, P. M., Palmer, K. L., Guan, Z., Siegenthaler, J. A., & Doran, K. S. (2024) · Science Advances · doi:10.1126/sciadv.adn7848 · Cited by 17 · see citing works
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The diverse actions of cytoskeletal vimentin in bacterial infection and host defense
Miao, C., Zhao, S., Etienne‐Manneville, S., & Jiu, Y. (2023) · Journal of Cell Science · doi:10.1242/jcs.260509 · Cited by 14 · see citing works
Vimentin Is an Attachment Receptor for Mycoplasma pneumoniae P1 Protein
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Cross-talk between Vimentin and autophagy regulates blood-testis barrier disruption induced by cadmium
Chen, N., Wan, X., Wang, M., Li, Y., Wang, X., Zeng, L., Zhou, J., Zhang, Y., Cheng, S., & Shen, Y. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.123625 · Cited by 13 · see citing works
Breaking the fortress: a mechanistic review of meningitis-causing bacteria breaching tactics in blood brain barrier
Quan, Y., Wang, Y., Gao, S., Yuan, S., Song, S., Liu, B., & Wang, Y. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02248-2 · Cited by 13 · see citing works
Molecular Characteristics of IS 1216 Carrying Multidrug Resistance Gene Cluster in Serotype III/Sequence Type 19 Group B Streptococcus
Zhi, Y., Ji, H. J., Jung, J., Byun, E. B., Kim, W. S., Lin, S. M., Lim, S., Jang, A.-Y., Choi, M. J., Ahn, K. B., et al. (2021) · mSphere · doi:10.1128/msphere.00543-21 · Cited by 12 · see citing works
The molecular biophysics of extracellular vimentin and its role in pathogen–host interactions
Parvanian, S., Coelho‐Rato, L. S., Eriksson, J., & Patteson, A. E. (2023) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2023.102233 · Cited by 11 · see citing works
Vimentin cage – A double-edged sword in host anti-infection defense
Zhao, S., Miao, C., Gao, X., Li, Z., Eriksson, J., & Jiu, Y. (2024) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2023.102317 · Cited by 11 · see citing works
Extracellular vimentin as a modulator of the immune response and an important player during infectious diseases
Suprewicz, Ł., Zakrzewska, M., Okła, S., Głuszek, K., Sadzyńska, A., Deptuła, P., Fiedoruk, K., & Bucki, R. (2024) · Immunology and Cell Biology · doi:10.1111/imcb.12721 · Cited by 11 · see citing works
Current research update on group B streptococcal infection related to obstetrics and gynecology
Liu, Y., & Ai, H. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1395673 · Cited by 11 · see citing works
Streptococcus intermedius : an underestimated pathogen in brain infection?
Gil, E., Hatcher, J., Saram, S. D., Guy, R. L., Lamagni, T. L., & Brown, J. (2024) · Future Microbiology · doi:10.1080/17460913.2024.2423524 · Cited by 11 · see citing works
Structure-Function Characterization of Streptococcus intermedius Surface Antigen Pas
Mieher, J. L., Schormann, N., Wu, R., Patel, M., Purushotham, S., Wu, H., Scoffield, J. A., & Deivanayagam, C. C. S. (2021) · Journal of Bacteriology · doi:10.1128/jb.00175-21 · Cited by 11 · see citing works
Uncovering the role of cytoskeleton proteins in the formation of neutrophil extracellular traps
Du, C., Cai, N., Dong, J., Xu, C., Wang, Q., Zhang, Z., Li, J., Huang, C., & Ma, T. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110607 · Cited by 10 · see citing works
Bacterial and host factors involved in zoonotic Streptococcal meningitis
Ma, J., Wu, H., Ma, Z., & Wu, Z. (2024) · Microbes and Infection · doi:10.1016/j.micinf.2024.105335 · Cited by 10 · see citing works
Targeting the BspC-vimentin interaction to develop anti-virulence therapies during Group B streptococcal meningitis
Manzer, H. S., Villarreal, R. I., & Doran, K. S. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010397 · Cited by 10 · see citing works
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The Group B Streptococcal Adhesin BspC Interacts with Host Cytokeratin 19 To Promote Colonization of the Female Reproductive Tract
Manzer, H. S., Nguyen, D. T., Park, J. Y., Park, N., Seo, K. S., Thornton, J. A., Nobbs, A. H., & Doran, K. S. (2022) · mBio · doi:10.1128/mbio.01781-22 · Cited by 10 · see citing works
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Different Involvement of Vimentin during Invasion by Listeria monocytogenes at the Blood–Brain and the Blood–Cerebrospinal Fluid Barriers In Vitro
Banović, F., Schulze, S., Mraheil, M. A., Hain, T., Chakraborty, T., Orian‐Rousseau, V., Moroniak, S., Weiß, C., Ishikawa, H., Schroten, H., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112908 · Cited by 9 · see citing works
The Clinical and Genetic Characteristics of Streptococcus agalactiae Meningitis in Neonates
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Mechanisms and Manifestations of Group B Streptococcus Meningitis in Newborns
Alexander, N. G., Cutts, W. D., Hooven, T. A., & Kim, B. J. (2025) · Journal of the Pediatric Infectious Diseases Society · doi:10.1093/jpids/piae103 · Cited by 9 · see citing works
Brain Infection by Group B Streptococcus Induces Inflammation and Affects Neurogenesis in the Adult Mouse Hippocampus
Segklia, K., Matsas, R., & Papastefanaki, F. (2023) · Cells · doi:10.3390/cells12121570 · Cited by 9 · see citing works
Dissecting Streptococcus pyogenes interaction with human
Ijaz, M., Ameén, F., Alfoteih, Y., Shamim, S., Alshehri, W. A., & Murtaza, G. (2020) · Archives of Microbiology · doi:10.1007/s00203-020-01932-w · Cited by 8 · see citing works
Vimentin Regulates Chemokine Expression and NOD2 Activation in Brain Endothelium during Group B Streptococcal Infection
Villarreal, R. I., Manzer, H. S., Keestra, A. M., & Doran, K. S. (2021) · Infection and Immunity · doi:10.1128/iai.00340-21 · Cited by 8 · see citing works
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Meningeal inflammation and arachnoid barrier breakdown in a mouse model of neonatal bacterial meningitis
Kim, S., Joyce, L. R., Brady, A., Spencer, B. L., Pawlikowski, B. T., Derk, J., Doran, K. S., & Siegenthaler, J. A. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.118141 · Cited by 6 · see citing works
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How BspC from Streptococcus agalactiae Interacts with Host Vimentin during Meningitis
Beninati, C., Famà, A., & Teti, G. (2019) · Trends in Microbiology · doi:10.1016/j.tim.2019.07.001 · Cited by 5 · see citing works
Polymorphonuclear Leukocyte Transendothelial Migration Proceeds at Blood-Brain Barrier in Neonatal Meningitis
Niu, Z., Chen, Y., & Zhang, K. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00969 · Cited by 5 · see citing works
Streptococcus agalactiae (Group B Streptococcus)
Wu, L. L., Dammann, A. N., & Ratner, A. J. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00081-2 · Cited by 4 · see citing works
Group B streptococcal infections
Ratner, A. J., Nizet, V., & Puopolo, K. M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-79525-8.00022-6 · Cited by 3 · see citing works
Comparative genomic analysis of hypervirulent group B streptococcus of ST12/serotype Ib suggests potential virulence factors
Zhou, K., Sun, Z., Sun, J., Xu, X., & Guan, M. (2025) · BMC Microbiology · doi:10.1186/s12866-025-04443-0 · Cited by 2 · see citing works
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Authors: Deng, L., Spencer, B. L., Holmes, J. A., Mu, R., Rego, S., Weston, T. A., Hu, Y., Sanches, G. F., Yoon, S., Park, N., Nagao, P. E., Jenkinson, H. F., Thornton, J. A., Seo, K. S., Nobbs, A. H., & Doran, K. S.
Affiliations: San Diego State University (US)
University of Colorado Anschutz (US)
University of Bristol (GB)
Mississippi State University (US)
Universidade do Estado do Rio de Janeiro (BR)
Corresponding author: Doran, Kelly S.
ORCID: Deng, Liwen
Spencer, Brady L.
Holmes, Joshua A.
Mu, Rong
Weston, Thomas A.
Hu, Yoonsung
Sanches, Glenda F.
Yoon, Sunghyun
Nagao, Prescilla E.
Jenkinson, Howard F.
Thornton, Justin A.
Seo, Keun Seok
Nobbs, Angela H.
Doran, Kelly S.
Venue: PLOS Pathogens
Publisher: Public Library of Science (PLoS)
Published: 2019-06-10
Volume: 15
Issue: 6
Pages: e1007848
ISSN: 1553-7366 (ISSN-L)
1553-7374
DOI: 10.1371/journal.ppat.1007848
PMC: PMC6586375
OpenAlex: W2949218991
Cited by: 74
References: 95
Citations by year: 2026: 7 · 2025: 4 · 2024: 11 · 2023: 14 · 2022: 14 · 2021: 10 · 2020: 9 · 2019: 5
FWCI: 8.69
Type: journal article
Language: en
Update notices: new_version (2019-06-20)
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: PLoS Pathogens (publishedVersion, cc-by)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Explore Bristol Research (publishedVersion, cc-by)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Figshare (submittedVersion, cc-by)
Bristol Research (University of Bristol) (submittedVersion, cc-by)
Funders: Mississippi State University
University of Bristol
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior ((Code 001))
National Institutes of Health
Anschutz Medical Campus, University of Colorado
National Institute of General Medical Sciences (P20GM103476)
National Institute of Allergy and Infectious Diseases (T32AI007405)
National Institute of Neurological Disorders and Stroke (R01NS051247)
National Institute of Dental and Craniofacial Research (R01DE016690)
Topics: Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Neonatal and Maternal Infections
Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Streptococcal Infections and Treatments
Keywords: Streptococcus agalactiae, vimentin, bacterial adhesion, brain endothelium, meningitis, host-pathogen interaction, neutrophil chemokines, neuroinflammation, Lactococcus lactis, bacterial virulence
MeSH terms: Animals, Antigens, Bacterial, Bacterial Proteins, Brain, Endothelium, Vascular, HeLa Cells, Humans, Male, Mice, Mutant Strains, Sheep, Streptococcal Infections, Streptococcus agalactiae, Vimentin, Meningitis, Bacterial, Mice

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The Group B Streptococcal surface antigen I/II protein, BspC, interacts with host vimentin to promote adherence to brain endothelium and inflammation during the pathogenesis of meningitis.

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