Identification of Burkholderia mallei and Burkholderia pseudomallei adhesins for human respiratory epithelial cells.

Balder, Rachel; Lipski, Serena; Lazarus, John J; Grose, William; Wooten, Ronald M; Hogan, Robert J; Woods, Donald E; Lafontaine, Eric R

doi:10.1186/1471-2180-10-250

Cited by 62Burkholderia infections and melioidosisBacterial Infections and VaccinesMicrobial infections and disease research

Identification of Burkholderia mallei and Burkholderia pseudomallei adhesins for human respiratory epithelial cells.

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Balder, Rachel, Lipski, Serena, Lazarus, John J, Grose, William, Wooten, Ronald M, Hogan, Robert J, Woods, Donald E, Lafontaine, Eric R·2010·BMC Microbiology

DOI 10.1186/1471-2180-10-250PMC PMC2955633

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Abstract

BACKGROUND: Burkholderia pseudomallei and Burkholderia mallei cause the diseases melioidosis and glanders, respectively. A well-studied aspect of pathogenesis by these closely-related bacteria is their ability to invade and multiply within eukaryotic cells. In contrast, the means by which B. pseudomallei and B. mallei adhere to cells are poorly defined. The purpose of this study was to identify adherence factors expressed by these organisms. RESULTS: Comparative sequence analyses identified a gene product in the published genome of B. mallei strain ATCC23344 (locus # BMAA0649) that resembles the well-characterized Yersinia enterocolitica autotransporter adhesin YadA. The gene encoding this B. mallei protein, designated boaA, was expressed in Escherichia coli and shown to significantly increase adherence to human epithelial cell lines, specifically HEp2 (laryngeal cells) and A549 (type II pneumocytes), as well as to cultures of normal human bronchial epithelium (NHBE). Consistent with these findings, disruption of the boaA gene in B. mallei ATCC23344 reduced adherence to all three cell types by ~50%. The genomes of the B. pseudomallei strains K96243 and DD503 were also found to contain boaA and inactivation of the gene in DD503 considerably decreased binding to monolayers of HEp2 and A549 cells and to NHBE cultures.A second YadA-like gene product highly similar to BoaA (65% identity) was identified in the published genomic sequence of B. pseudomallei strain K96243 (locus # BPSL1705). The gene specifying this protein, termed boaB, appears to be B. pseudomallei-specific. Quantitative attachment assays demonstrated that recombinant E. coli expressing BoaB displayed greater binding to A549 pneumocytes, HEp2 cells and NHBE cultures. Moreover, a boaB mutant of B. pseudomallei DD503 showed decreased adherence to these respiratory cells. Additionally, a B. pseudomallei strain lacking expression of both boaA and boaB was impaired in its ability to thrive inside J774A.1 murine macrophages, suggesting a possible role for these proteins in survival within professional phagocytic cells. CONCLUSIONS: The boaA and boaB genes specify adhesins that mediate adherence to epithelial cells of the human respiratory tract. The boaA gene product is shared by B. pseudomallei and B. mallei whereas BoaB appears to be a B. pseudomallei-specific adherence factor.

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iTasser detected some homology to an adhesin, BoaA, from Burkholderia pseudomallei with structure 3s6l.
“iTasser detected some homology to an adhesin, BoaA, from Burkholderia pseudomallei with structure 3s6l (Balder et al., 2010).”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Balder et al., 2010
The Discussion (page unavailable) identifies BoaA as an adhesin in B. pseudomallei, supporting the cited identification. The paper does not report an iTasser homology result or associate BoaA with structure 3s6l; its Methods describe other sequence and structure-prediction tools. (LLM, conf=0.86)
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Seçkin Serdar, A. R. U. N., Neubauer, H., Gürel, A., Ayyildiz, G., Kuşçu, B., Yeşildere, T., Meyer, H. E., & Hermanns, W. (1999) · Veterinary Record · doi:10.1136/vr.144.10.255 · Cited by 72 · see citing works
:Medical Aspects of Biological Warfare
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Patrick, C. C., KIMURA, A. E., Jackson, M. A., Hermanstorfer, L., Hood, A., McCracken, G. H., & Hansen, E. J. (1987) · Infection and Immunity · doi:10.1128/iai.55.12.2902-2911.1987 · Cited by 67 · see citing works
Identification and characterization of a two-component regulatory system involved in invasion of eukaryotic cells and heavy-metal resistance in Burkholderia pseudomallei
Jones, A. L., DeShazer, D., & Woods, D. E. (1997) · Infection and Immunity · doi:10.1128/iai.65.12.4972-4977.1997 · Cited by 67 · see citing works
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Schell, M. A., Lipscomb, L., & DeShazer, D. (2008) · Journal of Bacteriology · doi:10.1128/jb.01735-07 · Cited by 65 · see citing works
Virulent Burkholderia pseudomallei is more efficient than avirulent Burkholderia thailandensis in invasion of and adherence to cultured human epithelial cells
Kespichayawattana, W., Intachote, P., Utaisincharoen, P., & Sirisinha, S. (2004) · Microbial Pathogenesis · doi:10.1016/j.micpath.2004.01.001 · Cited by 64 · see citing works
Biological weapons defense: infectious disease and counterbioterrorism.
Lindler, L. E., Lebeda, F. J., & Korch, G. W. (2004) · Humana Press eBooks · Cited by 64 · see citing works
Dosing Regimens of Cotrimoxazole (Trimethoprim-Sulfamethoxazole) for Melioidosis
Cheng, A. C., McBryde, E. S., Wuthiekanun, V., Chierakul, W., Amornchai, P., Day, N., White, N. J., & Peacock, S. J. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01301-08 · Cited by 62 · see citing works
Protease Activity, Secretion, Cell Entry, Cytotoxicity, and Cellular Targets of Secreted Autotransporter Toxin of Uropathogenic Escherichia coli
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Strategies toward vaccines againstBurkholderia malleiandBurkholderia pseudomallei
Bondi, S. K., & Goldberg, J. B. (2008) · Expert Review of Vaccines · doi:10.1586/14760584.7.9.1357 · Cited by 61 · see citing works
Molecular Characterization of a Secreted Enzyme with Phospholipase B Activity from Moraxella bovis
Farn, J. L., Strugnell, R. A., Hoyne, P. A., Michalski, W. P., & Tennent, J. M. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.22.6717-6720.2001 · Cited by 59 · see citing works
Moraxella catarrhalisStrain O35E Expresses Two Filamentous Hemagglutinin-Like Proteins That Mediate Adherence to Human Epithelial Cells
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Fate of a Burkholderia pseudomallei Lipopolysaccharide Mutant in the Mouse Macrophage Cell Line RAW 264.7: Possible Role for the O-Antigenic Polysaccharide Moiety of Lipopolysaccharide in Internalization and Intracellular Survival
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Identification of the acid phosphatase (acpA) gene homologues in pathogenic and non-pathogenic Burkholderia spp. facilitates TnphoA mutagenesis
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Hag Directly Mediates the Adherence ofMoraxella catarrhalisto Human Middle Ear Cells
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Self-citation
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DeShazer, D. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00946.x · Cited by 52 · see citing works
Temperature-Regulated Microcolony Formation by<i>Burkholderia pseudomallei</i>Requires<i>pilA</i>and Enhances Association with Cultured Human Cells
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Cloning of the class D beta-lactamase gene from Burkholderia pseudomallei and studies on its expression in ceftazidime-susceptible and -resistant strains
Niumsup, P. R. (2002) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkf165 · Cited by 48 · see citing works
Biological weapons defense, infectious diseases, and counterbioterrorism
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Tiyawisutsri, R., Holden, M. T. G., Tumapa, S., Rengpipat, S., Clarke, S. R., Foster, S. J., Nierman, W. C., Day, N., & Peacock, S. J. (2007) · BMC Microbiology · doi:10.1186/1471-2180-7-19 · Cited by 39 · see citing works
ATP-binding cassette systems in Burkholderia pseudomallei and Burkholderia mallei
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Cloning and Expression of Class A β-Lactamase Gene blaA BPS in Burkholderia pseudomallei
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The Animal Pathogen-Like Type III Secretion System Is Required for the Intracellular Survival of Burkholderia mallei within J774.2 Macrophages
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Hag Mediates Adherence ofMoraxella catarrhalisto Ciliated Human Airway Cells
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Self-citation
Identification of Gene Products Involved in Biofilm Production by Moraxella catarrhalis ETSU-9 In Vitro
Pearson, M. M., & Hansen, E. J. (2007) · Infection and Immunity · doi:10.1128/iai.01347-06 · Cited by 33 · see citing works
Regions important for the adhesin activity of Moraxella catarrhalis Hag
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Bacterial Adhesins: Determinants of Microbial Colonization and Pathogenicity
Geme, J. W. S. (1997) · Advances in Pediatrics · doi:10.1016/s0065-3101(24)00048-3 · Cited by 31 · see citing works
Characterization of a laboratory-generated variant of BPS beta-lactamase from Burkholderia pseudomallei that hydrolyses ceftazidime
Ho, P. (2002) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkf208 · Cited by 29 · see citing works
Medical Aspects of Biological Warfare
Platteborze, P. L. (2009) · Military review · Cited by 27 · see citing works
Involvement of the MyD88-independent pathway in controlling the intracellular fate ofBurkholderia pseudomalleiinfection in a mouse macrophage cell line (RAW 264.7)
Tangsudjai, S., Pudla, M., Limposuwan, K., Woods, D. E., Sirisinha, S., & Utaisincharoen, P. (2010) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2010.00205.x · Cited by 20 · see citing works
Self-citation
Identification of aMoraxella catarrhalisgene that confers adherence to various human epithelial cell linesin vitro
Lipski, S. L., Holm, M. M., & Lafontaine, E. R. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00549.x · Cited by 16 · see citing works
Self-citation
A UspA2H-Negative Variant of Moraxella catarrhalis Strain O46E Has a Deletion in a Homopolymeric Nucleotide Repeat Common to uspA2H Genes
Wang, W., Pearson, M. M., Attia, A. S., Blick, R. J., & Hansen, E. J. (2007) · Infection and Immunity · doi:10.1128/iai.00609-06 · Cited by 14 · see citing works
Entry into host cells by Legionella
Mustapha, M. S. (2002) · Frontiers in bioscience · doi:10.2741/samrakan · Cited by 10 · see citing works

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Melioidosis
Wiersinga, W. J., Virk, H. S., Torres, A. G., Currie, B. J., Peacock, S. J., Dance, D. A. B., & Limmathurotsakul, D. (2018) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.107 · Cited by 686 · see citing works
Strategies for Intracellular Survival of Burkholderia pseudomallei
Allwood, E. M., Devenish, R. J., Prescott, M., Adler, B., & Boyce, J. D. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00170 · Cited by 121 · see citing works
Pathogenicity and virulence of Burkholderia pseudomallei
Bzdyl, N. M., Moran, C. L., Bendo, J. B., & Sarkar‐Tyson, M. (2022) · Virulence · doi:10.1080/21505594.2022.2139063 · Cited by 65 · see citing works
Melioidosis: molecular aspects of pathogenesis
Stone, J. K., DeShazer, D., Brett, P. J., & Burtnick, M. N. (2014) · Expert Review of Anti-infective Therapy · doi:10.1586/14787210.2014.970634 · Cited by 64 · see citing works
Intracellular replication of the well-armed pathogen Burkholderia pseudomallei
Willcocks, S., Denman, C. C., Atkins, H. S., & Wren, B. W. (2016) · Current Opinion in Microbiology · doi:10.1016/j.mib.2015.11.007 · Cited by 55 · see citing works
Autotransporters and Their Role in the Virulence of Burkholderia pseudomallei and Burkholderia mallei
Adler, N. R. L., Stevens, J. M., Stevens, M. P., & Galyov, E. E. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00151 · Cited by 44 · see citing works
Mechanisms of Disease: Host-Pathogen Interactions between Burkholderia Species and Lung Epithelial Cells
David, J., Bell, R. E., & Clark, G. C. (2015) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2015.00080 · Cited by 39 · see citing works
Use of a Safe, Reproducible, and Rapid Aerosol Delivery Method to Study Infection by Burkholderia pseudomallei and Burkholderia mallei in Mice
Lafontaine, E. R., Zimmerman, S. M., Shaffer, T. L., Michel, F. J., Gao, X., & Hogan, R. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076804 · Cited by 30 · see citing works
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Identification of a Predicted Trimeric Autotransporter Adhesin Required for Biofilm Formation of Burkholderia pseudomallei
Adler, N. R. L., Dean, R. E., Saint, R. J., Stevens, M. P., Prior, J. L., Atkins, T. P., & Galyov, E. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079461 · Cited by 29 · see citing works
Characterization of an autotransporter adhesin protein shared by Burkholderia mallei and Burkholderia pseudomallei
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Functional Characterization of Burkholderia pseudomallei Trimeric Autotransporters
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Betaproteobacteria are predominant in drinking water: are there reasons for concern?
Ferro, P., Vaz‐Moreira, I., & Manaia, C. M. (2019) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2019.1680602 · Cited by 26 · see citing works
Antibodies against In Vivo -Expressed Antigens Are Sufficient To Protect against Lethal Aerosol Infection with Burkholderia mallei and Burkholderia pseudomallei
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Systematic Mutagenesis of Genes Encoding Predicted Autotransported Proteins of Burkholderia pseudomallei Identifies Factors Mediating Virulence in Mice, Net Intracellular Replication and a Novel Protein Conferring Serum Resistance
Adler, N. R. L., Stevens, M. P., Dean, R. E., Saint, R. J., Pankhania, D., Prior, J. L., Atkins, T. P., Kessler, B., Nithichanon, A., Lertmemongkolchai, G., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0121271 · Cited by 21 · see citing works
Twenty years of paradigm-breaking studies of taxonomy and symbiotic nitrogen fixation by beta-rhizobia, and indication of Brazil as a hotspot of Paraburkholderia diversity
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Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis
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Genetic diversity and transmission patterns of Burkholderia pseudomallei on Hainan island, China, revealed by a population genomics analysis
Zheng, H., Qin, J., Chen, H., Hu, H., Zhang, X., Yang, C., Wu, Y., Li, Y., Li, S., Kuang, H.-H., et al. (2021) · Microbial Genomics · doi:10.1099/mgen.0.000659 · Cited by 17 · see citing works
The Peptidoglycan-associated lipoprotein Pal contributes to the virulence of Burkholderia mallei and provides protection against lethal aerosol challenge
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The Autotransporter BpaB Contributes to the Virulence of Burkholderia mallei in an Aerosol Model of Infection
Zimmerman, S. M., Michel, F. J., Hogan, R. J., & Lafontaine, E. R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126437 · Cited by 14 · see citing works
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Burkholderia mallei and Burkholderia pseudomallei stimulate differential inflammatory responses from human alveolar type II cells (ATII) and macrophages
Lu, R. Q., Popov, V. L., Patel, J. G., & Eaves-Pyles, T. D. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00165 · Cited by 14 · see citing works
Genomic diversity of resistant and virulent factors of Burkholderia pseudomallei clinical strains recovered from Guangdong using whole genome sequencing
Shafiq, M., Ke, B., Li, X., Mi, Z., Yuan, Y., He, D., Deng, X., & Jiao, X. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.980525 · Cited by 12 · see citing works
Mannitol promotes adherence of an outbreak strain of Burkholderia multivorans via an exopolysaccharide-independent mechanism that is associated with upregulation of newly identified fimbrial and afimbrial adhesins
Denman, C. C., & Brown, A. R. (2013) · Microbiology · doi:10.1099/mic.0.064832-0 · Cited by 12 · see citing works
An Evolutionary Arms Race Between Burkholderia pseudomallei and Host Immune System: What Do We Know?
Chomkatekaew, C., Boonklang, P., Sangphukieo, A., & Chewapreecha, C. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.612568 · Cited by 11 · see citing works
Novel gain of function approaches for vaccine candidate identification in Burkholderia pseudomallei
Dowling, A. J. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00139 · Cited by 10 · see citing works
The Current Status of Extracellular Polymeric Substances Produced by Burkholderia pseudomallei
Mangalea, M. R., Borlee, G. I., & Borlee, B. R. (2017) · Current Tropical Medicine Reports · doi:10.1007/s40475-017-0118-2 · Cited by 10 · see citing works
Burkholderia mallei and Glanders
Khakhum, N., Tapia, D., & Torres, A. G. (2019) · Springer eBooks · doi:10.1007/978-3-030-03071-1_7 · Cited by 9 · see citing works
Host and Pathogen Communication in the Respiratory Tract: Mechanisms and Models of a Complex Signaling Microenvironment
Berry, S. B., Haack, A. J., Theberge, A. B., Brighenti, S., & Svensson, M. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.00537 · Cited by 6 · see citing works
Comprehensive genome analysis of Burkholderia contaminans SK875, a quorum-sensing strain isolated from the swine
Kim, E., Jung, H.-I., Park, S. H., Kim, H., & Kim, S. (2023) · AMB Express · doi:10.1186/s13568-023-01537-8 · Cited by 6 · see citing works
Burkholderia pseudomallei and Burkholderia mallei
Inglis, T. J. J., & Merritt, A. J. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397169-2.00042-1 · Cited by 6 · see citing works
Identification of Burkholderia pseudomallei Genes Induced During Infection of Macrophages by Differential Fluorescence Induction
Jitprasutwit, S., Jitprasutwit, N., Hemsley, C. M., Onlamoon, N., Withatanung, P., Muangsombut, V., Vattanaviboon, P., Stevens, J. M., Ong, C., Stevens, M. P., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00072 · Cited by 6 · see citing works
Vaccine Development Against Melioidosis
Galeas‐Pena, M., & Morici, L. A. (2023) · Springer eBooks · doi:10.1007/978-3-031-24355-4_15 · Cited by 4 · see citing works
Transcriptome analysis of human monocytic cells infected with Burkholderia species and exploration of pentraxin-3 as part of the innate immune response against the organisms
Aschenbroich, S. A., Lafontaine, E. R., López, M. C., Baker, H. V., & Hogan, R. J. (2019) · BMC Medical Genomics · doi:10.1186/s12920-019-0575-7 · Cited by 4 · see citing works
Self-citation
A virulence activator of a surface attachment protein in Burkholderia pseudomallei acts as a global regulator of other membrane-associated virulence factors
Sun, Z., Heacock-Kang, Y., McMillan, I., Cabanas, D., Zarzycki‐Siek, J., & Hoang, T. T. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1063287 · Cited by 3 · see citing works
Molecular Characterization of Putative Virulence Determinants inBurkholderia pseudomallei
Puah, S. M., Puthucheary, S. D., Wang, J. T., Pan, Y., & Chua, K. H. (2014) · The Scientific World JOURNAL · doi:10.1155/2014/590803 · Cited by 3 · see citing works
The C‐terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network
Kiessling, A. R., Harris, S. A., Weimer, K., Wells, G., & Goldman, A. (2022) · Molecular Microbiology · doi:10.1111/mmi.14953 · Cited by 2 · see citing works
Genome sequence of two novel virulent clinical strains of Burkholderia pseudomallei isolated from acute melioidosis cases imported to Israel from India and Thailand
Cohen-Gihon, I., Zaide, G., Amit, S., Zohar, I., Schwartz, O., Maor‬‏, ‪., Israeli, O., Bilinsky, G., Israeli, M., Lazar, S., et al. (2024) · BMC Genomic Data · doi:10.1186/s12863-024-01225-x · Cited by 3 · see citing works
Burkholderia pseudomallei
Pflughoeft, K. J., Hau, D., Thorkildson, P., & AuCoin, D. P. (2019) · Springer eBooks · doi:10.1007/978-3-030-03071-1_8 · Cited by 2 · see citing works
Prophages Present in Acinetobacter pittii Influence Bacterial Virulence, Antibiotic Resistance, and Genomic Rearrangements
Zhu, R., & Mathur, V. (2022) · PHAGE · doi:10.1089/phage.2021.0014 · Cited by 2 · see citing works
Proteomic-based identification of novel EV-derived protein antibodies biomarkers for melioidosis diagnosis
Luo, N., Tan, J., Li, X., Wang, Y., Zhang, T., Chen, C., Liu, L., Song, X., Pei, H., Wang, B., et al. (2025) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0013543 · Cited by 1 · see citing works
The immune battle against Burkholderia pseudomallei in melioidosis progression
Verma, N., Srivastava, A., & Agarwal, V. C. (2026) · The Microbe · doi:10.1016/j.microb.2026.100721 · Cited by 1 · see citing works
A Novel Virulent Clinical Isolate of Burkholderia pseudomallei Imported from Thailand Exhibiting Resistance to Trimethoprim-Sulfamethoxazole
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Histopathological Effects of Burkholderia Mallei Isolated from Patients with Wound Infections on Mice
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respiratory epithelial cells
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Authors: Balder, R., Lipski, S., Lazarus, J. J., Grose, W., Wooten, R. M., Hogan, R. J., Woods, D. E., & Lafontaine, E. R.
Affiliations: University of Georgia (US)
University of Toledo (US)
University of Calgary (CA)
Corresponding author: Lafontaine, Eric R
ORCID: Wooten, Ronald M
Hogan, Robert J
Lafontaine, Eric R
Venue: BMC Microbiology
Publisher: Springer Science and Business Media LLC
Published: 2010-09-28
Volume: 10
Issue: 1
Pages: 250-250
ISSN: 1471-2180 (ISSN-L)
DOI: 10.1186/1471-2180-10-250
PMC: PMC2955633
OpenAlex: W2163750401
Cited by: 61
References: 111
Citations by year: 2026: 4 · 2025: 2 · 2024: 8 · 2023: 4 · 2022: 4 · 2021: 3 · 2020: 7 · 2019: 4 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 3 · 2014: 5 · 2013: 6 · 2012: 1
FWCI: 2.56
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: BMC Microbiology (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: University of Georgia
National Institutes of Health (5r01ai073452-04)
College of Veterinary Medicine, University of Georgia
National Institute of Allergy and Infectious Diseases (AI062775, R21AI062775, R01-AI073452)
Topics: Health Sciences › Medicine › Epidemiology › Burkholderia infections and melioidosis
Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
Life Sciences › Immunology and Microbiology › Microbiology › Microbial infections and disease research
Keywords: Burkholderia mallei, Burkholderia pseudomallei, bacterial adhesins, bacterial adhesion, airway epithelial cells, melioidosis, glanders, autophagy, phagocytosis, macrophages, gene disruption, alveolar epithelial cells, laryngeal epithelium
MeSH terms: Amino Acid Sequence, Animals, Cell Line, Epithelial Cells, Female, Genes, Bacterial, Humans, Mice, Inbred BALB C, Molecular Sequence Data, Species Specificity, Gene Expression Regulation, Bacterial, Burkholderia pseudomallei, Sequence Analysis, DNA, Adhesins, Bacterial, Burkholderia mallei, Mice

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Identification of Burkholderia mallei and Burkholderia pseudomallei adhesins for human respiratory epithelial cells.

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