Cited by 303Listeria monocytogenes in Food SafetyBiochemical and Structural CharacterizationBacterial Genetics and Biotechnology

The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.

Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin

Open access

Schubert, Wolf-Dieter, Urbanke, Claus, Ziehm, Thilo, Beier, Viola, Machner, Matthias P., Domann, Eugen, Wehland, Jürgen, Chakraborty, Trinad, Heinz, Dirk W.·2002·Cell

DOI 10.1016/s0092-8674(02)01136-4

Open this paper in CoChat — free account Open PDF

Abstract

Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian cells by inducing its own phagocytosis. The listerial protein internalin (InlA) mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. We present the crystal structures of the functional domain of InlA alone and in a complex with the extracellular, N-terminal domain of human E-cadherin (hEC1). The leucine rich repeat (LRR) domain of InlA surrounds and specifically recognizes hEC1. Individual interactions were probed by mutagenesis and analytical ultracentrifugation. These include Pro16 of hEC1, a major determinant for human susceptibility to L. monocytogenes infection that is essential for intermolecular recognition. Our studies reveal the structural basis for host tro-pism of this bacterium and the molecular deception L. monocytogenes employs to exploit the E-cadherin system.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/s0092-8674(02)01136-4

Cites

55 of 55 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
Improved methods for building protein models in electron density maps and the location of errors in these models
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877
The atomic structure of protein-protein recognition sites 1 1Edited by A. R. Fersht
Conte, L. L., Chothia, C., & Janin, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2439 · Cited by 1,967
The leucine-rich repeat as a protein recognition motif
Kobe, B. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(01)00266-4 · Cited by 1,720

Show all 55 references

Research works printed but not linked: 3

Brünger, 1998, Crystallography & NMR system, Acta Crystallogr., D54, 905
CCP4, 1994, The CCP4 (Collaborative Computational Project 4) suite, Acta Crystallogr. D, 50, 760
Nicholls, 1993, Grasp, Biophys. J., 64, A166

Sorted by citations

Items 201–300 of 303

Pathogen and Toxin Entry - How Pathogens and Toxins Induce and Harness Endocytotic Mechanisms
Eierhoff, T., Stechmann, B., & Rmer, W. (2012) · InTech eBooks · doi:10.5772/45946 · Cited by 13
Resveratrol-Schiff Base Hybrid Compounds with Selective Antibacterial Activity: Synthesis, Biological Activity, and Computational Study
Sánchez‐González, R., Leyton, P., Aguilar, L. F., Reyna‐Jeldes, M., Coddou, C., Díaz, K., & Mellado, M. (2022) · Microorganisms · doi:10.3390/microorganisms10081483 · Cited by 13
Immunoinformatics Insights into the Internalin A and B Proteins to Design a Multi-Epitope Subunit Vaccine for L. monocytogenes
Asadollahi, P., Pakzad, I., Sadeghifard, N., Ghafourian, S., Kazemian, H., Kaviar, V. H., Fattahi, R., & Kalani, B. S. (2022) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-021-10359-w · Cited by 13
Classes and functions of Listeria monocytogenes surface proteins.
Dziadek, B. R., Dzitko, K., & Długońska, H. (2004) · PubMed · Cited by 13
Listeria InlB Expedites Vacuole Escape and Intracellular Proliferation by Promoting Rab7 Recruitment via Vps34
Cain, R. J., Scortti, M., Monzó, H. J., & Vázquez‐Boland, J. A. (2023) · mBio · doi:10.1128/mbio.03221-22 · Cited by 14
Anti-InlA single-domain antibodies that inhibit the cell invasion of Listeria monocytogenes
Yamazaki, T., Nagatoishi, S., Yamawaki, T., Nozawa, T., Matsunaga, R., Nakakido, M., Caaveiro, J. M. M., Nakagawa, I., & Tsumoto, K. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105254 · Cited by 12
Is the Exoproteome Important for Bacterial Pathogenesis? Lessons Learned from Interstrain Exoprotein Diversity in Listeria monocytogenes Grown at Different Temperatures
Cabrita, P., Trigo, M. J., Ferreira, R. B., & Brito, L. (2014) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2013.0151 · Cited by 12
Sedimentation Velocity Method in the Analytical Ultracentrifuge for the Study of Protein-Protein Interactions
Urbanke, C., Witte, G., & Curth, U. (2005) · Methods in molecular biology · doi:10.1385/1-59259-912-5:101 · Cited by 12
Self-citation
Invasive Pathway of Listeria Ivanovii in Human Amnion-Derived Wish Cells
Ammendolia, M. G., Superti, F., Bertuccini, L., Chiarini, F., Conte, M. P., Cipriani, D., Seganti, L., & Longhi, C. (2007) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463200702000309 · Cited by 12
Biofilm Formation, Motility, and Virulence of Listeria monocytogenes Are Reduced by Deletion of the Gene lmo0159, a Novel Listerial LPXTG Surface Protein
Shi, W., Zhang, Q., Li, H., Du, D., Xun, M., Wang, J., Jiang, J., Liu, C., Kou, L., & Ren, J. (2024) · Microorganisms · doi:10.3390/microorganisms12071354 · Cited by 11
A strong correlation between consensus sequences and unique super secondary structures in leucine rich repeats
Batkhishig, D., Enkhbayar, P., Kretsinger, R. H., & Matsushima, N. (2020) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25876 · Cited by 11
Antimicrobial effect of spore-forming probiotics Bacillus laterosporus and Bacillus megaterium against Listeria monocytogenes
Rajabi, S., Darban‐Sarokhalil, D., Tabatabaei, R. R., & Hosseini, F. (2020) · Archives of Microbiology · doi:10.1007/s00203-020-02004-9 · Cited by 11
An Internalin A Probe-Based Genosensor forListeria monocytogenesDetection and Differentiation
Bifulco, L., Ingianni, A., & Pompei, R. (2013) · BioMed Research International · doi:10.1155/2013/640163 · Cited by 11
LrrA, a novel leucine-rich repeat protein involved in cytoskeleton remodeling, is required for multicellular morphogenesis in Dictyostelium discoideum
Liu, C.-I., Cheng, T., Chen, S.-Z., Huang, Y.-C., & Chang, W. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.05.045 · Cited by 11
Rational Design of a Robust G-Quadruplex Aptamer as an Inhibitor to Alleviate Listeria monocytogenes Infection
Chen, X., Chang, Y., Ye, M., Wang, Z., Wu, S., & Duan, N. (2024) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.4c00496 · Cited by 10
Unveiling the Mutations and Conservation of InlA in Listeria monocytogenes
Li, L., Wang, Y., Pu, J., Chen, J., Liu, L., Mao, P., Sun, H., Luo, X., & Ye, C. (2024) · Microorganisms · doi:10.3390/microorganisms12030485 · Cited by 10
The leucine-rich repeats of LINGO-1 are not required for self-interaction or interaction with the amyloid precursor protein
Stein, T., & Walmsley, A. R. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.11.029 · Cited by 10
Pathogenomics: An updated European Research Agenda
Demuth, A., Aharonowitz, Y., Bachmann, T. T., Blum–Oehler, G., Buchrieser, C., Covacci, A., Dobrindt, U., Emödy, L., ENDE, A. V. D., Ewbank, J. J., et al. (2008) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2008.01.005 · Cited by 10
Self-citation
Exploitation of host cell cytoskeleton and signalling during Listeria monocytogenes entry into mammalian cells
Pizarro‐Cerdá, J., Sousa, S., & Cossart, P. (2004) · Comptes Rendus Biologies · doi:10.1016/j.crvi.2004.06.001 · Cited by 10
Investigating the effect of the inhibitory peptide on L.monocytogenes cell invasion: an in silico and in vitro study
Shivaee, A., Bahonar, S., Goudarzi, M., Hematian, A., Hajikhani, B., & Kalani, B. S. (2023) · Gut Pathogens · doi:10.1186/s13099-023-00576-7 · Cited by 9
Remodeling of theListeria monocytogenescell wall inside eukaryotic cells
del Portillo, F. G., & Pucciarelli, M. G. (2012) · Communicative & Integrative Biology · doi:10.4161/cib.18678 · Cited by 9
Characterization of the calcium-binding sites of Listeria monocytogenes InlB
Marino, M., Banerjee, M., Copp, J., Dramsi, S., Chapman, T. L., van der Geer, P., Cossart, P., & Ghosh, P. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.02.064 · Cited by 9
Crystal structure of Leptospira leucine-rich repeat 20 reveals a novel E-cadherin binding protein to induce NGAL expression in HK2 cells
Hsu, S., Chu, C.-H., Tian, Y., Chang, M., Chou, L.-F., Sun, Y., & Yang, C. (2020) · Biochemical Journal · doi:10.1042/bcj20200547 · Cited by 9
Screening of rationally designed oligopeptides for Listeria monocytogenes detection by means of a high density colorimetric microarray
Mascini, M., Guilbault, G. G., Monk, I. R., Hill, C., Carlo, M. D., & Compagnone, D. (2008) · Microchimica Acta · doi:10.1007/s00604-008-0035-0 · Cited by 9
Cell Biology of Invasion and Intracellular Growth byListeria monocytogenes
Pizarro‐Cerdá, J., & Cossart, P. (2014) · ASM Press eBooks · doi:10.1128/9781555816513.ch53 · Cited by 9
Crystal structure of an engineered YopM-InlB hybrid protein
Breitsprecher, D., Gherardi, E., Bleymüller, W. M., & Niemann, H. H. (2014) · BMC Structural Biology · doi:10.1186/1472-6807-14-12 · Cited by 8
The Shear Stress of Host Cell Invasion: Exploring the Role of Biomolecular Complexes
Tonkin, M. L., & Boulanger, M. J. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004539 · Cited by 8
Identification of internalin-A-like virulent proteins in Leishmania donovani
Mukherjee, I., Chakraborty, A., & Chakrabarti, S. (2016) · Parasites & Vectors · doi:10.1186/s13071-016-1842-5 · Cited by 8
Tip-enhanced Raman scattering of DNA aptamers for Listeria monocytogenes
He, S., Li, H., Gomes, C. L., & Voronine, D. V. (2018) · Biointerphases · doi:10.1116/1.5022303 · Cited by 7
The role of bacterial adhesion to epithelial cells in pathogenesis
Hauck, C. R. (2006) · Cambridge University Press eBooks · doi:10.1017/cbo9780511541537.006 · Cited by 6
Structures and Motifs Involved in Toll Signaling
Gangloff, M., Ludidi, P. L., & Gay, N. J. (2007) · Springer eBooks · doi:10.1007/0-387-27445-6_3 · Cited by 6
On the calculation of the binding force between decorin and collagen
Scott, P. G., Bishop, P. N., & Bella, J. (2006) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2006.01.011 · Cited by 6
Application of protein modeling and molecular simulation techniques in the field of food microbial contamination: principles, research status and future prospects
Cen, C., Yu, X., Shentu, X., Miao, S., & Wang, Y. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2519709 · Cited by 5
Porous and Planar Silicon Sensors
Mace, C. R., & Miller, B. L. (2008) · Springer eBooks · doi:10.1007/978-0-387-75113-9_11 · Cited by 5
Residual Variation Intolerance Score Detects Loci Under Selection in Neuroinvasive Listeria monocytogenes
Ferwerda, B., Maury, M. M., Brouwer, M. C., Hafner, L., ENDE, A. V. D., Bentley, S. D., Lecuit, M., & van de Beek, D. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02702 · Cited by 5
Retrospective Investigation of the Whole Genome of the Hypovirulent Listeria monocytogenes Strain of ST201, CC69, Lineage III, Isolated from a Piglet with Fatal Neurolisteriosis
Zaitsev, S. S., Khizhnyakova, M. A., & Anatolievna, F. V. (2022) · Microorganisms · doi:10.3390/microorganisms10071442 · Cited by 5
New insights into the putative role of leucine-rich repeat proteins of Leptospira interrogans and their participation in host cell invasion: an in silico analysis
Foltran, B. B., Gaspar, J. P., Silva, I. R. M., Pires, H. M., de Andrade, F. B., Costa, G. M., Paixao, J. E. L., Fernandes, L. G. V., Teixeira, A. F., & Nascimento, A. L. T. O. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1492352 · Cited by 4
Modeling the Anti-Adhesive Role of Punicalagin Against Listeria Monocytogenes from the Analysis of the Interaction Between Internalin A and E-Cadherin
Pedroni, L., Ghidini, S., Vázquez, J., Luque, F. J., & Dellafiora, L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157327 · Cited by 4
OF MICE AND MEN: DISSECTING THE INTERACTION BETWEEN LISTERIA MONOCYTOGENES INTERNALIN A AND E-CADHERIN
Genheden, S., & Eriksson, L. A. (2013) · Computational and Structural Biotechnology Journal · doi:10.5936/csbj.201303022 · Cited by 4
Invasion of Host Cells by Listeria monocytogenes
Pizarro‐Cerdá, J., & Cossart, P. (2007) · Springer eBooks · doi:10.1007/978-0-387-49376-3_8 · Cited by 4
Comparative Genomics and Evolution of Virulence
Barbuddhe, S. B., Hain, T., & Chakraborty, T. (2008) · CRC Press eBooks · doi:10.1201/9781420051414.ch10 · Cited by 3
Self-citation
Control strategies for Listeria monocytogenes in ready-to-eat foods and on food contact surfaces
Saini, J. K. (2012) · K-State Research Exchange (Kansas State University) · Cited by 3
Connecting chemical and biological properties to identify new functional materials: A study on Trifolium nigrescens extracts
Terzić, M., Zengin, G., Mocan, A., Frumuzachi, O., Çetiz, M. V., Caprioli, G., Acquaticci, L., Angeloni, S., Şenkardeş, İ., Saka, E., et al. (2025) · Industrial Crops and Products · doi:10.1016/j.indcrop.2025.121484 · Cited by 2
Bacterial Invasion into Non-Phagocytic Cells
Zhou, D. (2006) · Springer eBooks · doi:10.1007/978-0-387-32901-7_8 · Cited by 2
What Is the Problem with L. monocytogenes?
JORDAN, K. N., Leong, D., & Álvarez‐Ordóñez, A. (2015) · SpringerBriefs in food, health and nutrition · doi:10.1007/978-3-319-16286-7_2 · Cited by 2
Intraepithelial TCRαβ T Cells in Health and Disease
Cheroutre, H., & Lefrançois, L. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-415847-4.00035-5 · Cited by 2
Bases moléculaires du tropisme foetoplacentaire deListeria monocytogenes
Lecuit, M., & Cossart, P. (2005) · médecine/sciences · doi:10.1051/medsci/200521117 · Cited by 2
Designer Bugs: Structural Engineering to Build a Better Mouse Model
Bhaskaran, S. S., & Stebbins, C. E. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.05.009 · Cited by 2
Selection of Listeria monocytogenes InlA-Binding Peptides Using Phage Display—Novel Compounds for Diagnostic Applications?
Kenzel, J., Brüggemann, D., & Funke, S. A. (2022) · Applied Microbiology · doi:10.3390/applmicrobiol2040070 · Cited by 1
Molecular Characterization of Virulence-Related Genes in Listeria monocytogenes Isolated from Retail Meats in Sapporo, Japan
Yamazaki, T., Kosugi, Y., Makibe, F., & Matsuo, J. (2025) · Current Microbiology · doi:10.1007/s00284-025-04121-4 · Cited by 1
Clindamycin susceptibility and virulence characterization of Listeria monocytogenes strains isolated from meat and meat-processing environments
Pérez-Baltar, A., Hernández-Gelabert, B., López, P., Pérez-Boto, D., Arqués, J. L., Martı́nez-Suárez, J. V., & Montiel, R. (2026) · Frontiers in Microbiology · doi:10.3389/fmicb.2026.1833569 · Cited by 1
Coupling Far-Western Blotting with Peptide Microarrays Reveals Novel E-Cadherin Spore-Surface Ligands in Clostridioides difficile
Lopez-Garcia, O. K., Pizarro‐Guajardo, M., Kocurek, K. I., Rezenom, Y. H., & Paredes‐Sabja, D. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c01166 · Cited by 1
Extract of Listeria monocytogenes Induces the Apoptosis on the Human Promyelocytic Leukemia Cells, HL-60 Cells
Yang, E. J., Kim, D.-H., & Chang, J.-H. (2012) · The Journal of the Korea Contents Association · doi:10.5392/jkca.2012.12.02.348 · Cited by 1
Expression, purification and crystallization of the C-terminal LRR domain ofStreptococcus pyogenesprotein 0843
Haikarainen, T., Loimaranta, V., Prieto-Lopez, C., Battula, P., Finne, J., & Papageorgiou, A. C. (2013) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309113009664 · Cited by 1
Biochemie und Molekularbiologie 2003
Sträter, N., Maier, T., Skerra, A., Schürrle, K., & Schepers, U. (2004) · Nachrichten aus der Chemie · doi:10.1002/nadc.20040520309 · Cited by 1
Host Signaling Response to Adhesion of Bifidobacterium infantis
Gann, R. N. (2021) · Digital Commons - USU (Utah State University) · doi:10.26076/53d1-86bf · Cited by 1
Pathogenesis
Kuhn, M., Scortti, M. M., & V√°zquez-Boland, J. (2008) · CRC Press eBooks · doi:10.1201/9781420051414.ch4 · Cited by 1
Recent Advances in the Detection of Listeria monocytogenes
Adhikari, P., Florien, N., Gupta, S., & Kaushal, A. (2023) · Infectious diseases · doi:10.5772/intechopen.109948 · Cited by 2
Host and Pathogen Sensory Systems as Targets for Therapeutic Intervention
Kindrachuk, K. J. (2008) · University Library - University of Saskatchewan (University of Saskatchewan) · Cited by 1
The Issue of Species Specificity of Bacterial Infection, How to Address it Experimentally
Disson, O., Cossart, P., & Lecuit, M. (2010) · Wiley eBooks · doi:10.1002/9783527629664.ch12 · Cited by 1
Molecular Strategies for Active Host Cell Invasion by Apicomplexan Parasites
Tonkin, M. L. (2014) · UVic’s Research and Learning Repository (University of Victoria) · Cited by 1
The Effect Of Curcumin (Curcuma Longa) On Biofilm Formation And Surface Proteins Of Listeria Monocytogenes
Ruengvisesh, S. (2023) · ScholarWorks@UMassAmherst (University of Massachusetts Amherst) · doi:10.7275/2414617
Phenotyping of Host‐Pathogen Interactions in Mice
Lengeling, A., Müller, W., & Balling, R. (2006) · Wiley eBooks · doi:10.1002/9783527611942.ch8
Caracterização fenotípica e genotípica de Listeria monocytogenes isoladas de produtos cárneos crus comercializados no município de São Paulo
Rowlands, R. E. G. (2013) · doi:10.11606/t.9.2013.tde-29042014-163248
Molecular studies on streptococcal surface proteins
Waldemarsson, J. (2016) · Lund University Publications (Lund University)
Listeria invasion and spread in non-professional phagocytes
Southwick, F. S. (2006) · Cambridge University Press eBooks · doi:10.1017/cbo9780511541513.007
Sequence and structural determinants of strand swapping and binding affinity in cadherin domains
Posy, S. (n.d.) · ProQuest Demo Repository
Biomacromolecular Interactions, Assemblies and Machines: A Structural View
Heinz, D. W., Weiss, M. S., & Wendt, K. U. (2005) · ChemBioChem · doi:10.1002/cbic.200500459
Self-citation
Helical Parameters and Correlations of Tandem Leucine Rich Repeats in
Miyashita, H., Kretsinger, R. H., & Matsushima, N. (2014)
« Bases moléculaires du tropisme foetoplacentaire de Listeria monocytogenes / Molecular basis of Listeria monocytogenes fetoplacental tropism »
Lecuit, M., & Cossart, P. (2015)
Expressão diferencial da proteína internalina A em Listeria monocytogenes do sorotipo 4b de diferentes origens em caldos de enriquecimento seletivos e não-seletivos
da Silva, V. S. (2011) · Americanae (AECID Library)
Identifcation of new hosts-dependants factors in Bacillus cereus Molecular and functional characterization of IlsA, a surface protein essential for iron acquisition during infection
Daou, N. (2008)
The development of a molecular chaperone-based system to improve the heterologous production of Plasmodium falciparum AdoMetDC protein in E. coli.
Makhoba, X. H. (2011)
Biochemical and genetic characterization of IspC, an immunogenic surface protein with peptidoglycan hydrolase activity essential for virulence of Listeria monocytogenes
Wang, L. R. (2008) · uO Research (University of Ottawa) · doi:10.20381/ruor-13016
Investigating the potentially expanded target repertoire of murinized Internalin of Listeria monocytogenes
Ndima, D. (2016) · UpSpace Institutional Repository (University of Pretoria)
Expression and purification of internalin a ligand for internalization studies on non-professional phagocytic epithelial cells
Haddad, N. S. (2012) · SMARTech Repository (Georgia Institute of Technology)
Factors involved in the interaction between Bifidobacterium and the host mucosal surface
Nishiyama, K., & Mukai, T. (2018) · Japanese Journal of Lactic Acid Bacteria · doi:10.4109/jslab.29.13
La Malvasia istriana nel Triveneto. Risultati di un quinquennio di sperimentazione
Costacurta, A., Carraro, R., Niero, M., Molin, E., & Ostan, M. (2005) · Rivista di viticoltura e di enologia
Faculty Opinions recommendation of Listeria monocytogenes invades the epithelial junctions at sites of cell extrusion.
Lecuit, M. (2006) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1031162.365494
Structure Watch
(2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1044
Identification of factors involved in cell wall homeostasis and tolerance towards quaternary ammonium compounds in Listeria monocytogenes by genomic adaptation
Schulz, L. M. (2023) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9942
Development Of Sporobeads Coated With Hecad1/2 For Rapid Detection And Capturing Of Pathogenic Listeria Monocytogenes
Mohammadi, K., & Saris, P. E. J. (2023) · Proceedings of the World Congress on New Technologies · doi:10.11159/icbb23.114
Development of Sporobeads Coated With Hecad1/2 for Rapid Detection and Capturing Of Pathogenic Listeria Monocytogenes
Mohammadi, K., & Saris, P. E. J. (2023) · Journal of Biomedical Engineering and Biosciences · doi:10.11159/jbeb.2023.006
Investigating the Chemical–Biological Link in Ziziphora galinae Extracts for the Discovery of Novel Raw Materials via In Silico and In Vitro Assays
Korpayev, S., Çetiz, M. V., Glamočlija, J., Aničić, N., Gašić, U. M., Stojković, D. S., Agamuradov, M., Hamrayev, H., Dall’Acqua, S., & Zengin, G. (2025) · Food Science & Nutrition · doi:10.1002/fsn3.70875
VHH engineering and utilization for blood-brain barrier transport and anti-infectious diseases
Pérez, J. F., Asano, R., Uto, Y., Tsumoto, K., & Nakakido, M. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00069-8
Ultrasensitive detection of Listeria monocytogenes using a ratiometric fluorescence aptasensor in food products
Wang, F., Wu, H., Zhou, J., Li, H., Chen, S., Ye, Y., & Gong, J. (2025) · Journal of Future Foods · doi:10.1016/j.jfutfo.2025.09.005
Benzalkonium chloride adaptation induces filamentation in Listeria monocytogenes HL06 and enhances its growth in pasteurized milk and pork sausage at 4 °C
Yu, T., Jiang, X., Xu, X., Zhu, H., Hamilton, D. P., Qiu, S., Yin, J., & Jiang, X. (2026) · Food Microbiology · doi:10.1016/j.fm.2026.105083
Mécanismes d’acquisition du fer chez Bacillus cereus : rôles d’IlsA, du système Isd et des sidérophores dans l’assimilation du fer à partir de l’hème et de la ferritine
Khalil, E. A. (2013) · theses.fr (ABES) · doi:10.70675/540cf83dzc8bdz48f6zbb22zb3edbcabcb60
Understanding the hypovirulence and hypervirulence of listeria monocytogenes
Huang, L. (2019) · theses.fr (ABES) · doi:10.70675/38bcd895z8ee0z488ezb073za7bf06c78506
High thoughput study of biofilm and virulence in Listeria monocytogenes using innovative approaches
Lee, B.-H. (2019) · doi:10.70675/91d912d2z134ez4e14z8813z62231a785b7e · Cited by 1
Understanding virulence heterogeneity in Listeria monocytogenes
Hafner, L. (2021) · theses.fr (ABES) · doi:10.70675/46e92af9zd298z42dczbff5zf90528eb75f2
Contribution de la virulence de Listeria monocytogenes à sa dissémination dans l'hôte et l'environnement
Gaillard, J. (2023) · theses.fr (ABES) · doi:10.70675/8c3e1078zf49ez4662z893ezbf256ef32bc5
Understanding the Role of Internalin A and Internalin B in Listeria Monocytogenes Infection and Their Correlation with E-cad and C-met Receptors in the Intestine of Diarrhea Patients
Kadhim, H. A. Z., Al-Janabi, N., & Al-saad, N. F. (2026) · Medical Journal of Babylon · doi:10.4103/mjbl.mjbl_1439_23
Compositionally Biased Regions Within Structured Protein Domains
Harrison, P. (2026) · Biomolecules · doi:10.3390/biom16091222
Mechanobiological mechanisms of bacterial infection-host defense interactions
Wang, Y., Liu, G., Yang, L., Pan, X., Jiang, Y., Xu, G., Ren, Y., & Shi, Q. (2026) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2026.103347 · Cited by 1
Eucalyptus globulus and Cymbopogon flexuosus essential oils are possible candidates in mitigating L. monocytogenes pathogenesis: An in silico, in vitro and in vivo study in Drosophila melanogaster
Pereira, C. J. A., Cerveira, M. M., Rosado, R. P., Elvira, A. M. V. G., Garcia, V. P., ALBUQUERQUE, M. P. D., de Melo, L. G., Oliveira, M. D. C., Luchese, C., Paim, M. P., et al. (2026) · The Microbe · doi:10.1016/j.microb.2026.100754
Competitive Binding Mechanisms in Aptamer Cocktails against Escherichia coli O157: Insights from Experiments and Molecular Dynamics SimulationsPreprint
Shi, R., Cao, X., Liang, J., Huang, C., Cheng, L., Wang, X., Tu, Z., Hu, L., Qian, Q., Li, J., et al. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.7207679
Beyond steric blocking: Binding-induced interfacial reorganization enables signal-on impedimetric detection of Listeria monocytogenesPreprint
Song, Y., Krispin, R., Choe, Y. H., Okshtein, H., Hayouka, Z., Hurevich, M., Friedler, A., Cho, N., & Yitzchaik, S. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.7323521
Control of Listeria monocytogenes in fresh-cut chili peppers by bacteriocin paracin wx7-1: Activity, mechanism, and preservative efficacy
Bian, Y., Lin, J., Li, L., Zeng, P., Li, H., & Yi, L. (2026) · Physiological and Molecular Plant Pathology · doi:10.1016/j.pmpp.2026.103481
Hydrogen Bonds Determining the Conformation of Isolated Amino Acid Residues in Proteins: Re‐Examination of the Fully Extended C5 Structures
Vijayasarathy, M., & Balaram, P. (2026) · Journal of Peptide Science · doi:10.1002/psc.70131

Authors: Schubert, W.-D., Urbanke, C., Ziehm, T., Beier, V., Machner, M. P., Domann, E., Wehland, J., Chakraborty, T., & Heinz, D. W.
Affiliations: Helmholtz Centre for Infection Research (DE)
Medizinische Hochschule Hannover (DE)
Justus-Liebig-Universität Gießen (DE)
Corresponding author: Heinz, Dirk W.
ORCID: Schubert, Wolf-Dieter
Machner, Matthias P.
Domann, Eugen
Chakraborty, Trinad
Heinz, Dirk W.
Venue: Cell
Publisher: Elsevier BV
Published: 2002-12
Volume: 111
Issue: 6
Pages: 825-836
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(02)01136-4
OpenAlex: W2019496511
Cited by: 302
References: 55
Citations by year: 2026: 14 · 2025: 8 · 2024: 4 · 2023: 11 · 2022: 9 · 2021: 7 · 2020: 7 · 2019: 9 · 2018: 5 · 2017: 4 · 2016: 6 · 2015: 6 · 2014: 15 · 2013: 13 · 2012: 13
FWCI: 16.42
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3881 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Listeria monocytogenes in Food Safety
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: Listeria monocytogenes, internalin A, integrated nested Laplace approximation, E-cadherin, bacterial invasion, host cell receptors, leucine-rich repeat domain, protein-protein interaction, host tropism, host susceptibility to infection, epithelial cell adhesion, crystal structure
MeSH terms: Amino Acid Sequence, Bacterial Proteins, Cloning, Molecular, Cytoplasm, Humans, Intestinal Mucosa, Ions, Leucine, Listeria monocytogenes, Models, Molecular, Molecular Sequence Data, Mutation, Protein Binding, Ultracentrifugation, X-Ray Diffraction, Cadherins, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Crystallography, X-Ray

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks