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  1. Artikel ; Online: Structure of the Inmazeb cocktail and resistance to Ebola virus escape.

    Rayaprolu, Vamseedhar / Fulton, Benjamin O / Rafique, Ashique / Arturo, Emilia / Williams, Dewight / Hariharan, Chitra / Callaway, Heather / Parvate, Amar / Schendel, Sharon L / Parekh, Diptiben / Hui, Sean / Shaffer, Kelly / Pascal, Kristen E / Wloga, Elzbieta / Giordano, Stephanie / Negron, Nicole / Ni, Min / Copin, Richard / Atwal, Gurinder S /
    Franklin, Matthew / Boytz, Ruth Mabel / Donahue, Callie / Davey, Robert / Baum, Alina / Kyratsous, Christos A / Saphire, Erica Ollmann

    Cell host & microbe

    2023  Band 31, Heft 2, Seite(n) 260–272.e7

    Abstract: Monoclonal antibodies can provide important pre- or post-exposure protection against infectious disease for those not yet vaccinated or in individuals that fail to mount a protective immune response after vaccination. Inmazeb (REGN-EB3), a three-antibody ...

    Abstract Monoclonal antibodies can provide important pre- or post-exposure protection against infectious disease for those not yet vaccinated or in individuals that fail to mount a protective immune response after vaccination. Inmazeb (REGN-EB3), a three-antibody cocktail against Ebola virus, lessened disease and improved survival in a controlled trial. Here, we present the cryo-EM structure at 3.1 Å of the Ebola virus glycoprotein, determined without symmetry averaging, in a simultaneous complex with the antibodies in the Inmazeb cocktail. This structure allows the modeling of previously disordered portions of the glycoprotein glycan cap, maps the non-overlapping epitopes of Inmazeb, and illuminates the basis for complementary activities and residues critical for resistance to escape by these and other clinically relevant antibodies. We further provide direct evidence that Inmazeb protects against the rapid emergence of escape mutants, whereas monotherapies even against conserved epitopes do not, supporting the benefit of a cocktail versus a monotherapy approach.
    Mesh-Begriff(e) Humans ; Ebolavirus ; Hemorrhagic Fever, Ebola ; Antibodies, Viral ; Glycoproteins ; Epitopes ; Antibodies, Neutralizing
    Chemische Substanzen atoltivimab, maftivimab, and odesivimab-ebgn drug combination ; Antibodies, Viral ; Glycoproteins ; Epitopes ; Antibodies, Neutralizing
    Sprache Englisch
    Erscheinungsdatum 2023-01-27
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2278004-X
    ISSN 1934-6069 ; 1931-3128
    ISSN (online) 1934-6069
    ISSN 1931-3128
    DOI 10.1016/j.chom.2023.01.002
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies.

    Baum, Alina / Fulton, Benjamin O / Wloga, Elzbieta / Copin, Richard / Pascal, Kristen E / Russo, Vincenzo / Giordano, Stephanie / Lanza, Kathryn / Negron, Nicole / Ni, Min / Wei, Yi / Atwal, Gurinder S / Murphy, Andrew J / Stahl, Neil / Yancopoulos, George D / Kyratsous, Christos A

    Science (New York, N.Y.)

    2020  Band 369, Heft 6506, Seite(n) 1014–1018

    Abstract: Antibodies targeting the spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) present a promising approach to combat the coronavirus disease 2019 (COVID-19) pandemic; however, concerns remain that mutations can yield antibody ... ...

    Abstract Antibodies targeting the spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) present a promising approach to combat the coronavirus disease 2019 (COVID-19) pandemic; however, concerns remain that mutations can yield antibody resistance. We investigated the development of resistance against four antibodies to the spike protein that potently neutralize SARS-CoV-2, individually as well as when combined into cocktails. These antibodies remain effective against spike variants that have arisen in the human population. However, novel spike mutants rapidly appeared after in vitro passaging in the presence of individual antibodies, resulting in loss of neutralization; such escape also occurred with combinations of antibodies binding diverse but overlapping regions of the spike protein. Escape mutants were not generated after treatment with a noncompeting antibody cocktail.
    Mesh-Begriff(e) Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; Betacoronavirus/chemistry ; Betacoronavirus/genetics ; Betacoronavirus/immunology ; COVID-19 ; Coronavirus Infections/immunology ; Epitopes ; Genome, Viral ; Humans ; Mutant Proteins/chemistry ; Mutant Proteins/immunology ; Mutation ; Neutralization Tests ; Pandemics ; Pneumonia, Viral/immunology ; Protein Interaction Domains and Motifs ; SARS-CoV-2 ; Selection, Genetic ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology
    Chemische Substanzen Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Mutant Proteins ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-06-15
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.abd0831
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel: Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant

    Yurkovetskiy, Leonid / Wang, Xue / Pascal, Kristen E / Tomkins-Tinch, Christopher / Nyalile, Thomas P / Wang, Yetao / Baum, Alina / Diehl, William E / Dauphin, Ann / Carbone, Claudia / Veinotte, Kristen / Egri, Shawn B / Schaffner, Stephen F / Lemieux, Jacob E / Munro, James B / Rafique, Ashique / Barve, Abhi / Sabeti, Pardis C / Kyratsous, Christos A /
    Dudkina, Natalya V / Shen, Kuang / Luban, Jeremy

    Cell. 2020 Oct. 29, v. 183, no. 3

    2020  

    Abstract: The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide, reaching near fixation in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells ... ...

    Abstract The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide, reaching near fixation in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells rendered permissive by ectopic expression of human ACE2 or of ACE2 orthologs from various mammals, including Chinese rufous horseshoe bat and Malayan pangolin. D614G did not alter S protein synthesis, processing, or incorporation into SARS-CoV-2 particles, but D614G affinity for ACE2 was reduced due to a faster dissociation rate. Assessment of the S protein trimer by cryo-electron microscopy showed that D614G disrupts an interprotomer contact and that the conformation is shifted toward an ACE2 binding-competent state, which is modeled to be on pathway for virion membrane fusion with target cells. Consistent with this more open conformation, neutralization potency of antibodies targeting the S protein receptor-binding domain was not attenuated.
    Schlagwörter Manis javanica ; Rhinolophus ; Severe acute respiratory syndrome coronavirus 2 ; colon ; cryo-electron microscopy ; dissociation ; humans ; lungs ; membrane fusion ; neutralization ; protein synthesis ; virion ; viruses
    Sprache Englisch
    Erscheinungsverlauf 2020-1029
    Umfang p. 739-751.e8.
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel
    Anmerkung NAL-AP-2-clean
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2020.09.032
    Datenquelle NAL Katalog (AGRICOLA)

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  4. Artikel: Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant.

    Yurkovetskiy, Leonid / Wang, Xue / Pascal, Kristen E / Tomkins-Tinch, Christopher / Nyalile, Thomas / Wang, Yetao / Baum, Alina / Diehl, William E / Dauphin, Ann / Carbone, Claudia / Veinotte, Kristen / Egri, Shawn B / Schaffner, Stephen F / Lemieux, Jacob E / Munro, James / Rafique, Ashique / Barve, Abhi / Sabeti, Pardis C / Kyratsous, Christos A /
    Dudkina, Natalya / Shen, Kuang / Luban, Jeremy

    bioRxiv : the preprint server for biology

    2020  

    Abstract: The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and cells rendered permissive by ectopic ... ...

    Abstract The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and cells rendered permissive by ectopic expression of various mammalian ACE2 orthologs. Nonetheless, D614G affinity for ACE2 was reduced due to a faster dissociation rate. Assessment of the S protein trimer by cryo-electron microscopy showed that D614G disrupts a critical interprotomer contact and that this dramatically shifts the S protein trimer conformation toward an ACE2-binding and fusion-competent state. Consistent with the more open conformation, neutralization potency of antibodies targeting the S protein receptor-binding domain was not attenuated. These results indicate that D614G adopts conformations that make virion membrane fusion with the target cell membrane more probable but that D614G retains susceptibility to therapies that disrupt interaction of the SARS-CoV-2 S protein with the ACE2 receptor.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-07-15
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2020.07.04.187757
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant.

    Yurkovetskiy, Leonid / Wang, Xue / Pascal, Kristen E / Tomkins-Tinch, Christopher / Nyalile, Thomas P / Wang, Yetao / Baum, Alina / Diehl, William E / Dauphin, Ann / Carbone, Claudia / Veinotte, Kristen / Egri, Shawn B / Schaffner, Stephen F / Lemieux, Jacob E / Munro, James B / Rafique, Ashique / Barve, Abhi / Sabeti, Pardis C / Kyratsous, Christos A /
    Dudkina, Natalya V / Shen, Kuang / Luban, Jeremy

    Cell

    2020  Band 183, Heft 3, Seite(n) 739–751.e8

    Abstract: The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide, reaching near fixation in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells ... ...

    Abstract The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide, reaching near fixation in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells rendered permissive by ectopic expression of human ACE2 or of ACE2 orthologs from various mammals, including Chinese rufous horseshoe bat and Malayan pangolin. D614G did not alter S protein synthesis, processing, or incorporation into SARS-CoV-2 particles, but D614G affinity for ACE2 was reduced due to a faster dissociation rate. Assessment of the S protein trimer by cryo-electron microscopy showed that D614G disrupts an interprotomer contact and that the conformation is shifted toward an ACE2 binding-competent state, which is modeled to be on pathway for virion membrane fusion with target cells. Consistent with this more open conformation, neutralization potency of antibodies targeting the S protein receptor-binding domain was not attenuated.
    Mesh-Begriff(e) Angiotensin-Converting Enzyme 2 ; Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Viral/immunology ; Betacoronavirus/pathogenicity ; Betacoronavirus/physiology ; Betacoronavirus/ultrastructure ; COVID-19 ; Cells, Cultured ; Coronavirus Infections/virology ; Female ; Genetic Variation ; HEK293 Cells ; Humans ; Male ; Models, Molecular ; Pandemics ; Peptidyl-Dipeptidase A/metabolism ; Pneumonia, Viral/virology ; Protein Conformation ; Protein Processing, Post-Translational ; Receptors, Coronavirus ; Receptors, Virus/metabolism ; SARS-CoV-2 ; Species Specificity ; Spike Glycoprotein, Coronavirus/physiology ; Spike Glycoprotein, Coronavirus/ultrastructure
    Chemische Substanzen Antibodies, Monoclonal ; Antibodies, Viral ; Receptors, Coronavirus ; Receptors, Virus ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-09-15
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2020.09.032
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel: Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies

    Baum, Alina / Fulton, Benjamin O / Wloga, Elzbieta / Copin, Richard / Pascal, Kristen E / Russo, Vincenzo / Giordano, Stephanie / Lanza, Kathryn / Negron, Nicole / Ni, Min / Wei, Yi / Atwal, Gurinder S / Murphy, Andrew J / Stahl, Neil / Yancopoulos, George D / Kyratsous, Christos A

    Science

    Abstract: Antibodies targeting the spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) present a promising approach to combat the coronavirus disease 2019 (COVID-19) pandemic; however, concerns remain that mutations can yield antibody ... ...

    Abstract Antibodies targeting the spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) present a promising approach to combat the coronavirus disease 2019 (COVID-19) pandemic; however, concerns remain that mutations can yield antibody resistance. We investigated the development of resistance against four antibodies to the spike protein that potently neutralize SARS-CoV-2, individually as well as when combined into cocktails. These antibodies remain effective against spike variants that have arisen in the human population. However, novel spike mutants rapidly appeared after in vitro passaging in the presence of individual antibodies, resulting in loss of neutralization; such escape also occurred with combinations of antibodies binding diverse but overlapping regions of the spike protein. Escape mutants were not generated after treatment with a noncompeting antibody cocktail.
    Schlagwörter covid19
    Verlag WHO
    Dokumenttyp Artikel
    Anmerkung WHO #Covidence: #599039
    Datenquelle COVID19

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  7. Artikel: SARS-CoV-2 Spike protein variant D614G increases infectivity and retains sensitivity to antibodies that target the receptor binding domain

    Yurkovetskiy, Leonid / Pascal, Kristen E. / Tompkins-Tinch, Christopher / Nyalile, Thomas / Wang, Yetao / Baum, Alina / Diehl, William E. / Dauphin, Ann / Carbone, Claudia / Veinotte, Kristen / Egri, Shawn B. / Schaffner, Stephen F. / Lemieux, Jacob E. / Munro, James / Sabeti, Pardis C. / Kyratsous, Christos / Shen, Kuang / Luban, Jeremy

    Abstract: Virus genome sequence variants that appear over the course of an outbreak can be exploited to map the trajectory of the virus from one susceptible host to another While such variants are usually of no functional significance, in some cases they may allow ...

    Abstract Virus genome sequence variants that appear over the course of an outbreak can be exploited to map the trajectory of the virus from one susceptible host to another While such variants are usually of no functional significance, in some cases they may allow the virus to transmit faster, change disease severity, or confer resistance to antiviral therapies Since the discovery of SARS-CoV-2 as the cause of COVID-19, the virus has spread around the globe, and thousands of SARS-CoV-2 genomes have been sequenced The rate of sequence variation among SARS-CoV-2 isolates is modest for an RNA virus but the enormous number of human-to-human transmission events has provided abundant opportunity for selection of sequence variants Among these, the SARS-CoV-2 Spike protein variant, D614G, was not present in the presumptive common ancestor of this zoonotic virus, but was first detected in late January in Germany and China The D614G variant steadily increased in frequency and now constitutes >97% of isolates world-wide, raising the question whether D614G confers a replication advantage to SARS-CoV-2 Structural models predict that D614G would disrupt contacts between the S1 and S2 domains of the Spike protein and cause significant shifts in conformation Using single-cycle vectors we showed that D614G is three to nine-fold more infectious than the ancestral form on human lung and colon cell lines, as well as on other human cell lines rendered permissive by ectopic expression of human ACE2 and TMPRSS2, or by ACE2 orthologues from pangolin, pig, dog, or cat Nonetheless, monoclonal antibodies targeting the receptor binding domain of the SARS-CoV-2 Spike protein retain full neutralization potency These results suggest that D614G was selected for increased human-to-human transmission, that it contributed to the rapidity of SARS-CoV-2 spread around the world, and that it does not confer resistance to antiviral therapies targeting the receptor binding domain
    Schlagwörter covid19
    Verlag WHO
    Dokumenttyp Artikel
    Anmerkung WHO #Covidence: #637849
    Datenquelle COVID19

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  8. Artikel ; Online: Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies

    Baum, Alina / Fulton, Benjamin O. / Wloga, Elzbieta / Copin, Richard / Pascal, Kristen E. / Russo, Vincenzo / Giordano, Stephanie / Lanza, Kathryn / Negron, Nicole / Ni, Min / Wei, Yi / Atwal, Gurinder S. / Murphy, Andrew J. / Stahl, Neil / Yancopoulos, George D. / Kyratsous, Christos A.

    Science

    2020  , Seite(n) eabd0831

    Abstract: Antibodies targeting the spike protein of SARS-CoV-2 present a promising approach to combat the COVID19 pandemic; however, concerns remain that mutations can yield antibody resistance. We investigate the development of resistance against four antibodies ... ...

    Abstract Antibodies targeting the spike protein of SARS-CoV-2 present a promising approach to combat the COVID19 pandemic; however, concerns remain that mutations can yield antibody resistance. We investigate the development of resistance against four antibodies to the spike protein that potently neutralize SARS-CoV-2, individually as well as when combined into cocktails. These antibodies remain effective against spike variants that have arisen in the human population. However, novel spike mutants rapidly appeared following in vitro passaging in the presence of individual antibodies, resulting in loss of neutralization; such escape also occurred with combinations of antibodies binding diverse but overlapping regions of the spike protein. Importantly, escape mutants were not generated following treatment with a non-competing antibody cocktail.
    Schlagwörter Multidisciplinary ; covid19
    Sprache Englisch
    Verlag American Association for the Advancement of Science (AAAS)
    Erscheinungsland us
    Dokumenttyp Artikel ; Online
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.abd0831
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  9. Artikel: The monoclonal antibody combination REGEN-COV protects against SARS-CoV-2 mutational escape in preclinical and human studies

    Copin, Richard / Baum, Alina / Wloga, Elzbieta / Pascal, Kristen E / Giordano, Stephanie / Fulton, Benjamin O / Zhou, Anbo / Negron, Nicole / Lanza, Kathryn / Chan, Newton / Coppola, Angel / Chiu, Joyce / Ni, Min / Wei, Yi / Atwal, Gurinder S / Hernandez, Annabel Romero / Saotome, Kei / Zhou, Yi / Franklin, Matthew C /
    Hooper, Andrea T / McCarthy, Shane / Hamon, Sara / Hamilton, Jennifer D / Staples, Hilary M / Alfson, Kendra / Carrion, Ricardo / Ali, Shazia / Norton, Thomas / Somersan-Karakaya, Selin / Sivapalasingam, Sumathi / Herman, Gary A / Weinreich, David M / Lipsich, Leah / Stahl, Neil / Murphy, Andrew J / Yancopoulos, George D / Kyratsous, Christos A

    Cell. 2021 May 28,

    2021  

    Abstract: Monoclonal antibodies against SARS-CoV-2 are a clinically validated therapeutic option against COVID-19. Because rapidly emerging virus mutants are becoming the next major concern in the fight against the global pandemic, it is imperative that these ... ...

    Abstract Monoclonal antibodies against SARS-CoV-2 are a clinically validated therapeutic option against COVID-19. Because rapidly emerging virus mutants are becoming the next major concern in the fight against the global pandemic, it is imperative that these therapeutic treatments provide coverage against circulating variants and do not contribute to development of treatment-induced emergent resistance. To this end, we investigated the sequence diversity of the spike protein and monitored emergence of virus variants in SARS-COV-2 isolates found in COVID-19 patients treated with the two-antibody combination REGEN-COV, as well as in preclinical in vitro studies using single, dual, or triple antibody combinations, and in hamster in vivo studies using REGEN-COV or single monoclonal antibody treatments. Our study demonstrates that the combination of non-competing antibodies in REGEN-COV provides protection against all current SARS-CoV-2 variants of concern/interest and also protects against emergence of new variants and their potential seeding into the population in a clinical setting.
    Schlagwörter COVID-19 infection ; Severe acute respiratory syndrome coronavirus 2 ; hamsters ; humans ; monoclonal antibodies ; pandemic ; sequence diversity ; sowing ; therapeutics ; viruses
    Sprache Englisch
    Erscheinungsverlauf 2021-0528
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel
    Anmerkung Pre-press version
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2021.06.002
    Datenquelle NAL Katalog (AGRICOLA)

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  10. Artikel: Atopobium vaginae triggers an innate immune response in an in vitro model of bacterial vaginosis.

    Libby, Erika K / Pascal, Kristen E / Mordechai, Eli / Adelson, Martin E / Trama, Jason P

    Microbes and infection

    2008  Band 10, Heft 4, Seite(n) 439–446

    Abstract: Bacterial vaginosis is the most common vaginal disorder among women of reproductive age. The pathogenesis of bacterial vaginosis is poorly understood, but is defined by a transition in the vaginal flora from the predominant Lactobacillus species to other ...

    Abstract Bacterial vaginosis is the most common vaginal disorder among women of reproductive age. The pathogenesis of bacterial vaginosis is poorly understood, but is defined by a transition in the vaginal flora from the predominant Lactobacillus species to other bacterial species such as Atopobium vaginae and Gardnerella vaginalis. This change is associated with an increase in vaginal cytokine secretion. We hypothesize that vaginal epithelial cells respond to bacterial vaginosis-associated bacteria by triggering an innate immune response. We observed that vaginal epithelial cells secreted interleukin-6 and interleukin-8 in response to Atopobium vaginae and Gardnerella vaginalis, but not to Lactobacillus crispatus. Atopobium vaginae induced increased levels of interleukin-6 and interleukin-8 transcripts, as well as increased transcripts for the antimicrobial peptide beta-defensin 4. This innate immune response required live bacteria capable of protein synthesis in direct contact with vaginal epithelial cells. The response of vaginal epithelial cells was mediated by Toll-like receptor 2, required the adaptor protein MyD88, and involved activation of the NFkappaB signaling pathway. These results suggest that Atopobium vaginae stimulates an innate immune response from vaginal epithelial cells, leading to localized cytokine and defensin production, and possibly contributes to the pathogenesis of bacterial vaginosis.
    Mesh-Begriff(e) Actinobacteria/immunology ; Cell Line ; Epithelial Cells/immunology ; Epithelial Cells/microbiology ; Female ; Gardnerella vaginalis/immunology ; Gene Expression Profiling ; Humans ; Immunity, Innate ; Interleukin-6/metabolism ; Interleukin-8/metabolism ; Lactobacillus/immunology ; Myeloid Differentiation Factor 88/immunology ; NF-kappa B/immunology ; RNA, Messenger/biosynthesis ; Toll-Like Receptor 2/immunology ; Vaginosis, Bacterial/immunology ; Vaginosis, Bacterial/microbiology ; beta-Defensins/biosynthesis ; beta-Defensins/genetics
    Chemische Substanzen DEFB4A protein, human ; Interleukin-6 ; Interleukin-8 ; MYD88 protein, human ; Myeloid Differentiation Factor 88 ; NF-kappa B ; RNA, Messenger ; Toll-Like Receptor 2 ; beta-Defensins
    Sprache Englisch
    Erscheinungsdatum 2008-04
    Erscheinungsland France
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1465093-9
    ISSN 1769-714X ; 1286-4579
    ISSN (online) 1769-714X
    ISSN 1286-4579
    DOI 10.1016/j.micinf.2008.01.004
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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