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  1. AU="David B. Volkin"
  2. AU="Hancock, Brandon"
  3. AU="Gatesy, Samuel W M"
  4. AU="Chénard, Caroline"
  5. AU="Krishna Chinthapalli"
  6. AU="Eneyda Secada Cárdenas"
  7. AU="Talbot, Nick"
  8. AU="Perez-Shibayama, Christian"
  9. AU="Melissa M. Mills"
  10. AU="Goli, Haneesha"
  11. AU="Viviana Falcón-Cama"
  12. AU="Januschek, Friederike"
  13. AU="Bonilla-Aldana, D. Katterine"
  14. AU="Stix, Michael S"
  15. AU="Xiao, Bing"
  16. AU="Algattas, Hanna N"
  17. AU="Ihm, M"
  18. AU="Nivelo, Luis A"
  19. AU="Nirja Kaka"
  20. AU="Bahnă, Adriana Florina"
  21. AU="Wen, Changchun"
  22. AU="Nizami, Sarea Islam Nuha"
  23. AU="Douglas J Kelly"
  24. AU=Kingston Elizabeth V
  25. AU="Jyoti Nepal"
  26. AU="González, Ana M Martín"

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  1. Artikel ; Online: Nanoalum Formulations Containing Aluminum Hydroxide and CpG 1018 TM Adjuvants

    Sakshi Bajoria / Ozan S. Kumru / Jennifer Doering / Katherine Berman / Greta Van Slyke / Anneka Prigodich / Sergio A. Rodriguez-Aponte / Harry Kleanthous / J. Christopher Love / Nicholas J. Mantis / Sangeeta B. Joshi / David B. Volkin

    Vaccines, Vol 11, Iss 1030, p

    The Effect on Stability and Immunogenicity of a Recombinant SARS-CoV-2 RBD Antigen

    2023  Band 1030

    Abstract: Aluminum-salt vaccine adjuvants (alum) are commercially available as micron-sized particles with varying chemical composition and crystallinity. There are reports of enhanced adjuvanticity when the alum’s particle size is reduced to the nanometer range. ... ...

    Abstract Aluminum-salt vaccine adjuvants (alum) are commercially available as micron-sized particles with varying chemical composition and crystallinity. There are reports of enhanced adjuvanticity when the alum’s particle size is reduced to the nanometer range. Previously, we demonstrated that a recombinant receptor-binding domain (RBD)-based COVID-19 vaccine candidate (RBD-J; RBD-L452K-F490W) formulated with aluminum hydroxide (Alhydrogel ®

    AH) and CpG 1018™ (CpG) adjuvants induced potent neutralizing antibody responses in mice yet displayed instability during storage. In this work, we evaluated whether sonication of AH to the nanometer size range (nanoAH) could further enhance immunogenicity or improve storage stability of the above formulation. The addition of CpG to nanoAH (at mouse doses), however, caused re-agglomeration of nanoAH. AH-CpG interactions were evaluated by Langmuir binding isotherms and zeta potential measurements, and stabilized nanoAH + CpG formulations of RBD-J were then designed by (1) optimizing CpG:Aluminum dose ratios or (2) adding a small-molecule polyanion (phytic acid, PA). Compared with the micron-sized AH + CpG formulation, the two stabilized nanoAH + CpG formulations of RBD-J demonstrated no enhancement in SARS-CoV-2 pseudovirus neutralizing titers in mice, but the PA-containing nanoAH + CpG formulation showed improved RBD-J storage stability trends (at 4, 25, and 37 °C). The formulation protocols presented herein can be employed to evaluate the potential benefits of the nanoAH + CpG adjuvant combination with other vaccine antigens in different animal models.
    Schlagwörter nanoalum ; CpG 1018 ; adjuvant ; nanoparticle ; vaccine ; formulation ; Medicine ; R
    Thema/Rubrik (Code) 630
    Sprache Englisch
    Erscheinungsdatum 2023-05-01T00:00:00Z
    Verlag MDPI AG
    Dokumenttyp Artikel ; Online
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  2. Artikel ; Online: A C-terminal Pfs48/45 malaria transmission-blocking vaccine candidate produced in the baculovirus expression system

    Shwu-Maan Lee / John M. Hickey / Kazutoyo Miura / Sangeeta B. Joshi / David B. Volkin / C. Richter King / Jordan L. Plieskatt

    Scientific Reports, Vol 10, Iss 1, Pp 1-

    2020  Band 14

    Abstract: Abstract The Plasmodium falciparum gametocyte surface protein, Pfs48/45, is a potential target for malaria transmission-blocking vaccines. However, due to its size and complexity, expression of the full-length protein has been difficult, leading to focus ...

    Abstract Abstract The Plasmodium falciparum gametocyte surface protein, Pfs48/45, is a potential target for malaria transmission-blocking vaccines. However, due to its size and complexity, expression of the full-length protein has been difficult, leading to focus on the C-terminal six cysteine domain (6C) with the use of fusion proteins to facilitate expression and folding. In this study, we utilized the baculovirus system to evaluate the expression of three Pfs48/45 proteins including the full-length protein, the 6C domain fragment and the 6C domain mutant to prevent glycosylation. Expression of the recombinant Pfs48/45 proteins was conducted in super Sf9 cells combined with the use of tunicamycin to prevent N-glycosylation. The proteins were then evaluated as immunogens in mice to demonstrate the induction of functionally active polyclonal antibody responses as measured in the standard membrane feeding assay (SMFA). Only the 6C protein was found to exhibit significant transmission-reducing activity. Further characterization of the biologically active 6C protein demonstrated it was homogeneous in terms of size, charge, conformation, absence of glycosylation, and containing proper disulfide bond pairings. This study presents an alternative expression system, without the need of a fusion protein partner, for the Pfs48/45 6C protein fragment including further evaluation as a potential transmission-blocking vaccine candidate.
    Schlagwörter Medicine ; R ; Science ; Q
    Thema/Rubrik (Code) 500
    Sprache Englisch
    Erscheinungsdatum 2020-01-01T00:00:00Z
    Verlag Nature Publishing Group
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  3. Artikel: Structural Changes and Aggregation Mechanisms of Two Different Dimers of an IgG2 Monoclonal Antibody

    Zhang, Jun / Christopher Woods / David B. Volkin / Feng He / Mei Han / Michael J. Treuheit

    Biochemistry. 2018 Aug. 24, v. 57, no. 37

    2018  

    Abstract: Protein therapeutics, monoclonal antibodies (mAbs) in particular, are large, structurally complex molecules that are prone to numerous modes of degradation during their production and long-term storage. Physical degradation via protein aggregation is a ... ...

    Abstract Protein therapeutics, monoclonal antibodies (mAbs) in particular, are large, structurally complex molecules that are prone to numerous modes of degradation during their production and long-term storage. Physical degradation via protein aggregation is a major concern when developing protein therapeutic candidates for clinical use. A dimer is perhaps the simplest element of protein aggregation, and thus, a better understanding of protein dimers in terms of their structures, intermolecular interactions, and chemical nature will help in the development of rational strategies for reducing aggregation propensity. In this study, two different mAb dimers were generated from an IgG2 monoclonal antibody solution, i.e., a native dimer generated under long-term storage and a thermal dimer from a thermal stress condition. Both IgG2 dimers were characterized in terms of their chemical and physical properties, bioactivity, and conformational dynamics. The native IgG2 dimer was formed mainly through noncovalent association. It displayed minimal differences in biophysical properties and higher-order structure compared to the monomer yet showed compromised in vitro potency, likely because of steric hindrance. In contrast, the thermal IgG2 dimer was mainly disulfide-linked, but even so, no new non-native disulfide bonds were detected by peptide mapping. Two regions within the Fc-CH2 domain of the thermal IgG2 dimer exhibited significantly increased flexibility as measured by hydrogen–deuterium exchange mass spectrometry, and notably, these regions are connected by an intrachain disulfide bond under natively folded conditions. These findings provide a better understanding of dimer formation under long-term storage and thermal stress conditions for this IgG2 mAb, and possible aggregation mechanisms are discussed.
    Schlagwörter bioactive properties ; disulfide bonds ; immunoglobulin G ; mass spectrometry ; monoclonal antibodies ; peptide mapping ; physical properties ; storage time ; therapeutics ; thermal stress
    Sprache Englisch
    Erscheinungsverlauf 2018-0824
    Umfang p. 5466-5479.
    Erscheinungsort American Chemical Society
    Dokumenttyp Artikel
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.8b00575
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  4. Artikel ; Online: A ferritin-based COVID-19 nanoparticle vaccine that elicits robust, durable, broad-spectrum neutralizing antisera in non-human primates

    Payton A.-B. Weidenbacher / Mrinmoy Sanyal / Natalia Friedland / Shaogeng Tang / Prabhu S. Arunachalam / Mengyun Hu / Ozan S. Kumru / Mary Kate Morris / Jane Fontenot / Lisa Shirreff / Jonathan Do / Ya-Chen Cheng / Gayathri Vasudevan / Mark B. Feinberg / Francois J. Villinger / Carl Hanson / Sangeeta B. Joshi / David B. Volkin / Bali Pulendran /
    Peter S. Kim

    Nature Communications, Vol 14, Iss 1, Pp 1-

    2023  Band 13

    Abstract: Abstract While the rapid development of COVID-19 vaccines has been a scientific triumph, the need remains for a globally available vaccine that provides longer-lasting immunity against present and future SARS-CoV-2 variants of concern (VOCs). Here, we ... ...

    Abstract Abstract While the rapid development of COVID-19 vaccines has been a scientific triumph, the need remains for a globally available vaccine that provides longer-lasting immunity against present and future SARS-CoV-2 variants of concern (VOCs). Here, we describe DCFHP, a ferritin-based, protein-nanoparticle vaccine candidate that, when formulated with aluminum hydroxide as the sole adjuvant (DCFHP-alum), elicits potent and durable neutralizing antisera in non-human primates against known VOCs, including Omicron BQ.1, as well as against SARS-CoV-1. Following a booster ~one year after the initial immunization, DCFHP-alum elicits a robust anamnestic response. To enable global accessibility, we generated a cell line that can enable production of thousands of vaccine doses per liter of cell culture and show that DCFHP-alum maintains potency for at least 14 days at temperatures exceeding standard room temperature. DCFHP-alum has potential as a once-yearly (or less frequent) booster vaccine, and as a primary vaccine for pediatric use including in infants.
    Schlagwörter Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2023-04-01T00:00:00Z
    Verlag Nature Portfolio
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  5. Artikel ; Online: The Pfs230 N-terminal fragment, Pfs230D1+

    Shwu-Maan Lee / Yimin Wu / John M. Hickey / Kazutoyo Miura / Neal Whitaker / Sangeeta B. Joshi / David B. Volkin / C. Richter King / Jordan Plieskatt

    Malaria Journal, Vol 18, Iss 1, Pp 1-

    expression and characterization of a potential malaria transmission-blocking vaccine candidate

    2019  Band 13

    Abstract: Abstract Background Control and elimination of malaria can be accelerated by transmission-blocking interventions such as vaccines. A surface antigen of Plasmodium falciparum gametocytes, Pfs230, is a leading vaccine target antigen, and has recently ... ...

    Abstract Abstract Background Control and elimination of malaria can be accelerated by transmission-blocking interventions such as vaccines. A surface antigen of Plasmodium falciparum gametocytes, Pfs230, is a leading vaccine target antigen, and has recently progressed to experimental clinical trials. To support vaccine product development, an N-terminal Pfs230 antigen was designed to increase yield, as well as to improve antigen quality, integrity, and homogeneity. Methods A scalable baculovirus expression system was used to express the Pfs230D1+ construct (aa 552–731), which was subsequently purified and analysed. Pfs230D1+ was designed to avoid glycosylation and protease digestion, thereby potentially increasing homogeneity and stability. The resulting Pfs230D1+ protein was compared to a previous iteration of the Pfs230 N-terminal domain, Pfs230C1 (aa 443–731), through physiochemical characterization and in vivo analysis. The induction of functional antibody responses was confirmed via the standard membrane feeding assay (SMFA). Results Pfs230D1+ was produced and purified to an overall yield of 23 mg/L culture supernatant, a twofold yield increase over Pfs230C1. The Pfs230D1+ protein migrated as a single band via SDS-PAGE and was detected by anti-Pfs230C1 monoclonal antibodies. Evaluation by SDS-PAGE, chromatography (size-exclusion and reversed phase) and capillary isoelectric focusing demonstrated the molecule had improved homogeneity in terms of size, conformation, and charge. Intact mass spectrometry confirmed its molecular weight and that it was free of glycosylation, a key difference to the prior Pfs230C1 protein. The correct formation of the two intramolecular disulfide bonds was initially inferred by binding of a conformation specific monoclonal antibody and directly confirmed by LC/MS and peptide mapping. When injected into mice the Pfs230D1+ protein elicited antibodies that demonstrated transmission-reducing activity, via SMFA, comparable to Pfs230C1. Conclusion By elimination of an O-glycosylation site, a ...
    Schlagwörter Malaria ; Pfs230 ; Plasmodium falciparum ; Transmission-blocking vaccine ; Baculovirus ; Glycosylation ; Arctic medicine. Tropical medicine ; RC955-962 ; Infectious and parasitic diseases ; RC109-216
    Thema/Rubrik (Code) 570
    Sprache Englisch
    Erscheinungsdatum 2019-11-01T00:00:00Z
    Verlag BMC
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  6. Artikel: Combined semi-empirical screening and design of experiments (DOE) approach to identify candidate formulations of a lyophilized live attenuated tetravalent viral vaccine candidate

    Patel, Ashaben / David B. Volkin / Jill Livengood / Lee Smith / Linda Strange / Ozan Kumru / Paul Nelson / Ravi S. Shukla / Sangeeta B. Joshi / Steven M. Erb

    Vaccine. 2017,

    2017  

    Abstract: A combination experimental approach, utilizing semi-empirical excipient screening followed by statistical modeling using design of experiments (DOE), was undertaken to identify stabilizing candidate formulations for a lyophilized live attenuated ... ...

    Abstract A combination experimental approach, utilizing semi-empirical excipient screening followed by statistical modeling using design of experiments (DOE), was undertaken to identify stabilizing candidate formulations for a lyophilized live attenuated Flavivirus vaccine candidate. Various potential pharmaceutical compounds used in either marketed or investigative live attenuated viral vaccine formulations were first identified. The ability of additives from different categories of excipients, either alone or in combination, were then evaluated for their ability to stabilize virus against freeze-thaw, freeze-drying, and accelerated storage (25°C) stresses by measuring infectious virus titer. An exploratory data analysis and predictive DOE modeling approach was subsequently undertaken to gain a better understanding of the interplay between the key excipients and stability of virus as well as to determine which combinations were interacting to improve virus stability. The lead excipient combinations were identified and tested for stabilizing effects using a tetravalent mixture of viruses in accelerated and real time (2-8°C) stability studies. This work demonstrates the utility of combining semi-empirical excipient screening and DOE experimental design strategies in the formulation development of lyophilized live attenuated viral vaccine candidates.
    Schlagwörter additives ; experimental design ; Flavivirus ; freeze drying ; freeze-thaw cycles ; screening ; statistical models ; viral load ; viral vaccines ; viruses
    Sprache Englisch
    Umfang p. .
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    Anmerkung Pre-press version
    ZDB-ID 605674-x
    ISSN 1873-2518 ; 0264-410X
    ISSN (online) 1873-2518
    ISSN 0264-410X
    DOI 10.1016/j.vaccine.2017.04.086
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  7. Artikel: Development of a candidate stabilizing formulation for bulk storage of a double mutant heat labile toxin (dmLT) protein based adjuvant

    Toprani, Vishal M / C. Russell Middaugh / David B. Volkin / George A. Robertson / John M. Hickey / Neha Sahni / Sangeeta B. Joshi

    Vaccine. 2017,

    2017  

    Abstract: This work describes the formulation design and development of a novel protein based adjuvant, a double mutant of heat labile toxin (dmLT), based on knowledge of the protein’s structural integrity and physicochemical degradation pathways (as described ... ...

    Abstract This work describes the formulation design and development of a novel protein based adjuvant, a double mutant of heat labile toxin (dmLT), based on knowledge of the protein’s structural integrity and physicochemical degradation pathways (as described in the companion paper in this special issue of Vaccine). Various classes of pharmaceutical excipients were screened for their stabilizing effect on dmLT during exposure to thermal and agitation stresses as monitored by high throughput analytical assays for dmLT degradation. Sucrose, phosphate, sodium chloride, methionine and polysorbate-80 were identified as potential stabilizers that protected dmLT against either conformational destabilization, aggregation/particle formation or chemical degradation (e.g., Met oxidation and Lys glycation). Different combinations and concentrations of the selected stabilizers were then evaluated to further optimize dmLT stability while maintaining pharmaceutically acceptable ranges of solution pH and osmolality. The effect of multiple freeze-thaw (FT) cycles on the physical stability of candidate bulk formulations was also examined. Increasing the polysorbate-80 concentration to 0.1% in the lead candidate bulk formulation mitigated the loss of protein mass during FT. This formulation development study enabled the design of a new bulk formulation of the dmLT adjuvant and provides flexibility for future use in combination with a variety of different vaccine dosage forms with different antigens.
    Schlagwörter adjuvants ; agitation ; antigens ; chemical degradation ; drug formulations ; freeze-thaw cycles ; glycation ; heat ; methionine ; mutants ; osmolality ; oxidation ; pH ; phosphates ; sodium chloride ; stabilizers ; sucrose ; vaccines
    Sprache Englisch
    Umfang p. .
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    Anmerkung Pre-press version
    ZDB-ID 605674-x
    ISSN 1873-2518 ; 0264-410X
    ISSN (online) 1873-2518
    ISSN 0264-410X
    DOI 10.1016/j.vaccine.2017.03.101
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  8. Artikel: Challenges and opportunities of using liquid chromatography and mass spectrometry methods to develop complex vaccine antigens as pharmaceutical dosage forms

    Hickey, John M / C. Russell Middaugh / David B. Volkin / Neha Sahni / Ozan S. Kumru / Ronald T. Toth / Sangeeta B. Joshi

    Journal of chromatography. 2016 Oct. 01, v. 1032

    2016  

    Abstract: Liquid chromatographic methods, combined with mass spectrometry, offer exciting and important opportunities to better characterize complex vaccine antigens including recombinant proteins, virus-like particles, inactivated viruses, polysaccharides, and ... ...

    Abstract Liquid chromatographic methods, combined with mass spectrometry, offer exciting and important opportunities to better characterize complex vaccine antigens including recombinant proteins, virus-like particles, inactivated viruses, polysaccharides, and protein-polysaccharide conjugates. The current abilities and limitations of these physicochemical methods to complement traditional in vitro and in vivo vaccine potency assays are explored in this review through the use of illustrative case studies. Various applications of these state-of-the art techniques are illustrated that include the analysis of influenza vaccines (inactivated whole virus and recombinant hemagglutinin), virus-like particle vaccines (human papillomavirus and hepatitis B), and polysaccharide linked to protein carrier vaccines (pneumococcal). Examples of utilizing these analytical methods to characterize vaccine antigens in the presence of adjuvants, which are often included to boost immune responses as part of the final vaccine dosage form, are also presented. Some of the challenges of using chromatographic and LC–MS as physicochemical assays to routinely test complex vaccine antigens are also discussed.
    Schlagwörter adjuvants ; antigens ; case studies ; drug formulations ; hemagglutinins ; hepatitis B ; humans ; immune response ; influenza ; liquid chromatography ; mass spectrometry ; Papillomaviridae ; polysaccharides ; recombinant proteins ; viruses ; virus-like particle vaccines ; virus-like particles
    Sprache Englisch
    Erscheinungsverlauf 2016-1001
    Umfang p. 23-38.
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    ISSN 1570-0232
    DOI 10.1016/j.jchromb.2016.04.001
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  9. Artikel: Adsorption of recombinant poxvirus L1-protein to aluminum hydroxide/CpG vaccine adjuvants enhances immune responses and protection of mice from vaccinia virus challenge

    Xiao, Yuhong / C. Russell Middaugh / David B. Volkin / Edward Alexander / George W. Buchman / Sangeeta B. Joshi / Shyam Mehta / Stuart N. Isaacs / Yuhong Zeng

    Vaccine. 2013 Jan. 02, v. 31, no. 2

    2013  

    Abstract: The stockpiling of live vaccinia virus vaccines has enhanced biopreparedness against the intentional or accidental release of smallpox. Ongoing research on future generation smallpox vaccines is providing key insights into protective immune responses as ... ...

    Abstract The stockpiling of live vaccinia virus vaccines has enhanced biopreparedness against the intentional or accidental release of smallpox. Ongoing research on future generation smallpox vaccines is providing key insights into protective immune responses as well as important information about subunit-vaccine design strategies. For protein-based recombinant subunit vaccines, the formulation and stability of candidate antigens with different adjuvants are important factors to consider for vaccine design. In this work, a non-tagged secreted L1-protein, a target antigen on mature virus, was expressed using recombinant baculovirus technology and purified. To identify optimal formulation conditions for L1, a series of biophysical studies was performed over a range of pH and temperature conditions. The overall physical stability profile was summarized in an empirical phase diagram. Another critical question to address for development of an adjuvanted vaccine was if immunogenicity and protection could be affected by the interactions and binding of L1 to aluminum salts (Alhydrogel) with and without a second adjuvant, CpG. We thus designed a series of vaccine formulations with different binding interactions between the L1 and the two adjuvants, and then performed a series of vaccination-challenge experiments in mice including measurement of antibody responses and post-challenge weight loss and survival. We found that better humoral responses and protection were conferred with vaccine formulations when the L1-protein was adsorbed to Alhydrogel. These data demonstrate that designing vaccine formulation conditions to maximize antigen–adjuvant interactions is a key factor in smallpox subunit-vaccine immunogenicity and protection.
    Schlagwörter adsorption ; aluminum ; aluminum hydroxide ; antigens ; humoral immunity ; immune response ; mice ; pH ; physical phases ; salts ; subunit vaccines ; temperature ; vaccine adjuvants ; vaccine development ; Vaccinia virus ; viruses ; weight loss
    Sprache Englisch
    Erscheinungsverlauf 2013-0102
    Umfang p. 319-326.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 605674-x
    ISSN 1873-2518 ; 0264-410X
    ISSN (online) 1873-2518
    ISSN 0264-410X
    DOI 10.1016/j.vaccine.2012.11.007
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