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  1. AU="Yongfeng Fan"
  2. AU="Merghani, M."
  3. AU="Shankar, Archana"
  4. AU="Lau, Wilma"
  5. AU="Milosević-Stevanović, Jelena" AU="Milosević-Stevanović, Jelena"
  6. AU="Levens, Cassandra"
  7. AU=Gerdes Hans-Hermann
  8. AU="Johnson, Abigail N"
  9. AU="Zheng, Yuanyuan"
  10. AU="Xia, Fan"
  11. AU="Wilson, Louis G"
  12. AU="Aubertin, Perrine"
  13. AU=Remmel Ariana
  14. AU="Tabbo, Agnese"
  15. AU="Chen, Linyi"
  16. AU="Milovanovic, Marija"
  17. AU="Vaught, Emma K"
  18. AU="Chapelle, Caroline"
  19. AU="Schmelzeisen, R"
  20. AU=Sillanaukee P AU=Sillanaukee P
  21. AU="Meyler, Shanique"

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  1. Artikel ; Online: Seismic Response Study of L-Shaped Frame Structure with Magnetorheological Dampers

    Jiangtao You / Yang Yang / Yongfeng Fan / Xiangcheng Zhang

    Applied Sciences, Vol 12, Iss 5976, p

    2022  Band 5976

    Abstract: To analyze the multi-dimensional seismic mitigation performance and the torsional vibration characteristic of an L-shaped frame structure with a magnetorheological damper (MRD). Firstly, the mechanical property of the MRD is experimentally studied. Then, ...

    Abstract To analyze the multi-dimensional seismic mitigation performance and the torsional vibration characteristic of an L-shaped frame structure with a magnetorheological damper (MRD). Firstly, the mechanical property of the MRD is experimentally studied. Then, the calculation models of the L-shaped frame structure without and with MRDs are found through theoretical analysis, and the programs of the calculation models are compiled. Finally, the time history responses of the calculation models are calculated during the excitation of bi-directional seismic wave; the responses of displacement, acceleration, story drift ratio, shear force and bending moment and torsional vibration are then compared and analyzed. The results show that by adjusting the current, the damping force provided by the MRD can be adjusted continuously in the range of 3.1 to 120 kN. The compiled calculation model programs of the L-shaped frame structure without and with MRDs can effectively simulate the multi-dimensional seismic response of the structure. Reasonable arrangement of MR dampers can effectively reduce the displacement, acceleration, shear force, bending moment, multi-dimensional vibration, and torsional vibration response of L-shaped frame structures.
    Schlagwörter magnetorheological damper ; seismic response ; story drift ratio ; shear force ; bending moment ; torsional vibration ; Technology ; T ; Engineering (General). Civil engineering (General) ; TA1-2040 ; Biology (General) ; QH301-705.5 ; Physics ; QC1-999 ; Chemistry ; QD1-999
    Thema/Rubrik (Code) 621
    Sprache Englisch
    Erscheinungsdatum 2022-06-01T00:00:00Z
    Verlag MDPI AG
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  2. Artikel ; Online: Multicolor fluorescence activated cell sorting to generate humanized monoclonal antibody binding seven subtypes of BoNT/F.

    Yongfeng Fan / Zhengda Sun / Fraser Conrad / Weihua Wen / Lequn Zhao / Jianlong Lou / Yu Zhou / Shauna Farr-Jones / James D Marks

    PLoS ONE, Vol 17, Iss 9, p e

    2022  Band 0273512

    Abstract: Generating specific monoclonal antibodies (mAbs) that neutralize multiple antigen variants is challenging. Here, we present a strategy to generate mAbs that bind seven subtypes of botulinum neurotoxin serotype F (BoNT/F) that differ from each other in ... ...

    Abstract Generating specific monoclonal antibodies (mAbs) that neutralize multiple antigen variants is challenging. Here, we present a strategy to generate mAbs that bind seven subtypes of botulinum neurotoxin serotype F (BoNT/F) that differ from each other in amino acid sequence by up to 36%. Previously, we identified 28H4, a mouse mAb with poor cross-reactivity to BoNT/F1, F3, F4, and F6 and with no detectable binding to BoNT/F2, F5, or F7. Using multicolor labeling of the different BoNT/F subtypes and fluorescence-activated cell sorting (FACS) of yeast displayed single-chain Fv (scFv) mutant libraries, 28H4 was evolved to a humanized mAb hu6F15.4 that bound each of seven BoNT/F subtypes with high affinity (KD 5.81 pM to 659.78 pM). In contrast, using single antigen FACS sorting, affinity was increased to the subtype used for sorting but with a decrease in affinity for other subtypes. None of the mAb variants showed any binding to other BoNT serotypes or to HEK293 or CHO cell lysates by flow cytometry, thus demonstrating stringent BoNT/F specificity. Multicolor FACS-mediated antibody library screening is thus proposed as a general method to generate multi-specific antibodies to protein subtypes such as toxins or species variants.
    Schlagwörter Medicine ; R ; Science ; Q
    Thema/Rubrik (Code) 570
    Sprache Englisch
    Erscheinungsdatum 2022-01-01T00:00:00Z
    Verlag Public Library of Science (PLoS)
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  3. Artikel ; Online: A three monoclonal antibody combination potently neutralizes multiple botulinum neurotoxin serotype F subtypes.

    Yongfeng Fan / Consuelo Garcia-Rodriguez / Jianlong Lou / Weihua Wen / Fraser Conrad / Wenwu Zhai / Theresa J Smith / Leonard A Smith / James D Marks

    PLoS ONE, Vol 12, Iss 3, p e

    2017  Band 0174187

    Abstract: Human botulism is primarily caused by botulinum neurotoxin (BoNT) serotypes A, B and E, with around 1% caused by serotype F (BoNT/F). BoNT/F comprises at least seven different subtypes with the amino acid sequence difference between subtypes as high as ... ...

    Abstract Human botulism is primarily caused by botulinum neurotoxin (BoNT) serotypes A, B and E, with around 1% caused by serotype F (BoNT/F). BoNT/F comprises at least seven different subtypes with the amino acid sequence difference between subtypes as high as 36%. The sequence differences present a significant challenge for generating monoclonal antibodies (mAbs) that can bind, detect and neutralize all BoNT/F subtypes. We used repertoire cloning of immune mouse antibody variable (V) regions and yeast display to generate a panel of 33 lead single chain Fv (scFv) mAbs that bound one or more BoNT/F subtypes with a median equilibrium dissociation constant (KD) of 4.06 × 10-9 M. By diversifying the V-regions of the lead mAbs and selecting for cross reactivity we generated five mAbs that bound each of the seven subtypes. Three scFv binding non-overlapping epitopes were converted to IgG that had KD for the different BoNT/F subtypes ranging from 2.2×10-8 M to 1.47×10-12 pM. An equimolar combination of the mAbs was able to potently neutralize BoNT/F1, F2, F4 and F7 in the mouse neutralization assay. The mAbs have potential utility as diagnostics capable of recognizing the known BoNT/F subtypes and could be developed as antitoxins to prevent and treat type F botulism.
    Schlagwörter Medicine ; R ; Science ; Q
    Thema/Rubrik (Code) 630
    Sprache Englisch
    Erscheinungsdatum 2017-01-01T00:00:00Z
    Verlag Public Library of Science (PLoS)
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  4. Artikel ; Online: Monoclonal Antibodies Targeting the Alpha-Exosite of Botulinum Neurotoxin Serotype/A Inhibit Catalytic Activity.

    Yongfeng Fan / Isin N Geren / Jianbo Dong / Jianlong Lou / Weihua Wen / Fraser Conrad / Theresa J Smith / Leonard A Smith / Mengfei Ho / Melissa Pires-Alves / Brenda A Wilson / James D Marks

    PLoS ONE, Vol 10, Iss 8, p e

    2015  Band 0135306

    Abstract: The paralytic disease botulism is caused by botulinum neurotoxins (BoNT), multi-domain proteins containing a zinc endopeptidase that cleaves the cognate SNARE protein, thereby blocking acetylcholine neurotransmitter release. Antitoxins currently used to ... ...

    Abstract The paralytic disease botulism is caused by botulinum neurotoxins (BoNT), multi-domain proteins containing a zinc endopeptidase that cleaves the cognate SNARE protein, thereby blocking acetylcholine neurotransmitter release. Antitoxins currently used to treat botulism neutralize circulating BoNT but cannot enter, bind to or neutralize BoNT that has already entered the neuron. The light chain endopeptidase domain (LC) of BoNT serotype A (BoNT/A) was targeted for generation of monoclonal antibodies (mAbs) that could reverse paralysis resulting from intoxication by BoNT/A. Single-chain variable fragment (scFv) libraries from immunized humans and mice were displayed on the surface of yeast, and 19 BoNT/A LC-specific mAbs were isolated by using fluorescence-activated cell sorting (FACS). Affinities of the mAbs for BoNT/A LC ranged from a KD value of 9.0×10-11 M to 3.53×10-8 M (mean KD 5.38×10-9 M and median KD 1.53×10-9 M), as determined by flow cytometry analysis. Eleven mAbs inhibited BoNT/A LC catalytic activity with IC50 values ranging from 8.3 ~73×10-9 M. The fine epitopes of selected mAbs were also mapped by alanine-scanning mutagenesis, revealing that the inhibitory mAbs bound the α-exosite region remote from the BoNT/A LC catalytic center. The results provide mAbs that could prove useful for intracellular reversal of paralysis post-intoxication and further define epitopes that could be targeted by small molecule inhibitors.
    Schlagwörter Medicine ; R ; Science ; Q
    Thema/Rubrik (Code) 572
    Sprache Englisch
    Erscheinungsdatum 2015-01-01T00:00:00Z
    Verlag Public Library of Science (PLoS)
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  5. Artikel ; Online: Monoclonal Antibodies that Inhibit the Proteolytic Activity of Botulinum Neurotoxin Serotype/B

    Yongfeng Fan / Jianbo Dong / Jianlong Lou / Weihua Wen / Fraser Conrad / Isin N. Geren / Consuelo Garcia-Rodriguez / Theresa J. Smith / Leonard A. Smith / Mengfei Ho / Melissa Pires-Alves / Brenda A. Wilson / James D. Marks

    Toxins, Vol 7, Iss 9, Pp 3405-

    2015  Band 3423

    Abstract: Existing antibodies (Abs) used to treat botulism cannot enter the cytosol of neurons and bind to botulinum neurotoxin (BoNT) at its site of action, and thus cannot reverse paralysis. However, Abs targeting the proteolytic domain of the toxin could ... ...

    Abstract Existing antibodies (Abs) used to treat botulism cannot enter the cytosol of neurons and bind to botulinum neurotoxin (BoNT) at its site of action, and thus cannot reverse paralysis. However, Abs targeting the proteolytic domain of the toxin could inhibit the proteolytic activity of the toxin intracellularly and potentially reverse intoxication, if they could be delivered intracellularly. As such, antibodies that neutralize toxin activity could serve as potent inhibitory cargos for therapeutic antitoxins against botulism. BoNT serotype B (BoNT/B) contains a zinc endopeptidase light chain (LC) domain that cleaves synaoptobrevin-2, a SNARE protein responsible for vesicle fusion and acetylcholine vesicle release. To generate monoclonal Abs (mAbs) that could reverse paralysis, we targeted the protease domain for Ab generation. Single-chain variable fragment (scFv) libraries from immunized mice or humans were displayed on yeast, and 19 unique BoNT/B LC-specific mAbs isolated by fluorescence-activated cell sorting (FACS). The equilibrium dissociation constants (KD) of these mAbs for BoNT/B LC ranged from 0.24 nM to 14.3 nM (mean KD 3.27 nM). Eleven mAbs inhibited BoNT/B LC proteolytic activity. The fine epitopes of selected mAbs were identified by alanine-scanning mutagenesis, revealing that inhibitory mAbs bound near the active site, substrate-binding site or the extended substrate-binding site. The results provide mAbs that could prove useful for intracellular reversal of paralysis and identify epitopes that could be targeted by small molecules inhibitors.
    Schlagwörter botulinum antitoxin ; inhibitory antibodies ; Botulinum neurotoxin serotype B ; alpha-exosite ; Medicine ; R
    Thema/Rubrik (Code) 572
    Sprache Englisch
    Erscheinungsdatum 2015-08-01T00:00:00Z
    Verlag MDPI AG
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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