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258 results on '"Asojo, Oluwatoyin A."'

1. Cultivating Success through Undergraduate Research Experience in a Historically Black College and University

Author

Ghebreyessus, Kesete, Ndip, Edmund M., Waddell, Michelle K., Asojo, Oluwatoyin A., and Njoki, Peter N.

Abstract

This reflective overview describes the benefits of participation in authentic undergraduate research for students at a Historically Black College and University (HBCU). The department of chemistry and biochemistry at Hampton University has an undergraduate research environment that empowers and fosters a success-oriented research experience for our diverse students. By engaging undergraduate students in research early in their careers, we successfully motivate students to make informed decisions about pursuing STEM careers and entering graduate schools with high confidence. Our structured undergraduate research experiences are created within an inclusive environment that instills a sense of belonging and recognizes the talent all our students bring to STEM. We reflect on our experiences using faculty-student research collaborations within nurturing support systems that leverage African American culture while setting high expectations to improve scientific skills and retain our HBCU students in STEM.

Published
2022
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8. The antischistosomal potential of GSK-J4, an H3K27 demethylase inhibitor: insights from molecular modeling, transcriptomics and in vitro assays

Author

Lobo-Silva, Jessica, Cabral, Fernanda J., Amaral, Murilo S., Miyasato, Patrícia A., de Freitas, Rafaela Paula, Pereira, Adriana S. A., Khouri, Mariana I., Barbosa, Mayra M. F., Ramos, Pablo I. P., Leite, Luciana C. C., Asojo, Oluwatoyin A., Nakano, Eliana, Verjovski-Almeida, Sergio, and Farias, Leonardo P.

Published
2020
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9. A novel multi-epitope recombinant protein elicits an antigen-specific CD8+ T cells response in Trypanosoma cruzi-infected mice

Author

González-López, Cristina, primary, Chen, Wen-Hsiang, additional, Alfaro-Chacón, Andrea, additional, Villanueva-Lizama, Liliana E., additional, Rosado-Vallado, Miguel, additional, Ramirez-Sierra, Maria Jesús, additional, Teh-Poot, Christian F., additional, Pollet, Jeroen, additional, Asojo, Oluwatoyin, additional, Jones, Kathryn M., additional, Hotez, Peter J., additional, Elena Bottazzi, Maria, additional, and Cruz-Chan, Julio Vladimir, additional

Published
2022
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14. Crystal structure of a hypothetical protein from Giardia lamblia. Corrigendum

Author

Beard, Dylan K., primary, Bristol, Seonna, additional, Cosby, Kayla, additional, Davis, Amber, additional, Manning, Courtney, additional, Perry, Lionel, additional, Snapp, Lauren, additional, Toy, Arian, additional, Wheeler, Kayla, additional, Young, Jeremy, additional, Staker, Bart, additional, Arakaki, Tracy L., additional, Abendroth, Jan, additional, Subramanian, Sandhya, additional, Edwards, Thomas E., additional, Myler, Peter J., additional, and Asojo, Oluwatoyin A., additional

Published
2022
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19. Crystal structures of FolM alternative dihydrofolate reductase 1 from Brucella suis and Brucella canis

Author

Porter, Imani, primary, Neal, Trinity, additional, Walker, Zion, additional, Hayes, Dylan, additional, Fowler, Kayla, additional, Billups, Nyah, additional, Rhoades, Anais, additional, Smith, Christian, additional, Smith, Kaelyn, additional, Staker, Bart L., additional, Dranow, David M., additional, Mayclin, Stephen J., additional, Subramanian, Sandhya, additional, Edwards, Thomas E., additional, Myler, Peter J., additional, and Asojo, Oluwatoyin A., additional

Published
2022
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24. Necator americanus Ancylostoma Secreted Protein-2 (Na-ASP-2) Binds an Ascaroside (ascr#3) in Its Fatty Acid Binding Site

Author

El Atab, Ola, Darwiche, Rabih, Truax, Nathanyal J., Schneiter, Roger, Hull, Kenneth G., Romo, Daniel, and Asojo, Oluwatoyin A.

Subjects
Chemistry, TAPs [testis specific proteins (Tpx)/antigen 5 (Ag5)/pathogenesis related-1 (PR-1)/Sc7], education, parasitic diseases, lipid binding, sperm coating protein (SCP), venom allergen-like (VAL), CAP [cysteine-rich secretory protein (CRISP)/antigen 5/pathogenesis related-1 (PR-1)], Original Research
Abstract

During their infective stages, hookworms release excretory-secretory (E-S) products, small molecules, and proteins to help evade and suppress the host's immune system. Small molecules found in E-S products of mammalian hookworms include nematode derived metabolites like ascarosides, which are composed of the sugar ascarylose linked to a fatty acid side chain. The most abundant proteins found in hookworm E-S products are members of the protein family known as Ancylostoma secreted protein (ASP). In this study, two ascarosides and their fatty acid moieties were synthesized and tested for in vitro binding to Na-ASP-2 using both a ligand competition assay and microscale thermophoresis. The fatty acid moieties of both ascarosides tested and ascr#3, an ascaroside found in rat hookworm E-S products, bind to Na-ASP-2's palmitate binding cavity. These molecules were confirmed to bind to the palmitate but not the sterol binding sites. An ascaroside, oscr#10, which is not found in hookworm E-S products, does not bind to Na-ASP-2. More studies are required to determine the structural basis of ascarosides binding by Na-ASP-2 and to understand the physiological significance of these observations.

Published
2020

31. Expression of the Necator americanus hookworm larval antigen Na-ASP-2 in Pichia pastoris and purification of the recombinant protein for use in human clinical trials

Author

Goud, Gaddam Narsa, Bottazzi, Maria Elena, Zhan, Bin, Mendez, Susana, Deumic, Vehid, Plieskatt, Jordan, Liu, Sen, Wang, Yan, Bueno, Lilian, Fujiwara, Ricardo, Samuel, Andre, Ahn, So Yeong, Solanki, Maneesha, Asojo, Oluwatoyin A., Wang, Jin, Bethony, Jeffrey M., Loukas, Alex, Roy, Michael, and Hotez, Peter J.

Published
2005
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34. Ligand binding properties of two Brugia malayi fatty acid and retinol (FAR) binding proteins and their vaccine efficacies against challenge infection in gerbils

Author

Zhan, Bin, primary, Arumugam, Sridhar, additional, Kennedy, Malcolm W., additional, Tricoche, Nancy, additional, Lian, Lu-Yun, additional, Asojo, Oluwatoyin A., additional, Bennuru, Sasisekhar, additional, Bottazzi, Maria Elena, additional, Hotez, Peter J., additional, Lustigman, Sara, additional, and Klei, Thomas R., additional

Published
2018
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36. The pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is a fatty acid-binding protein

Author

Darwiche, Rabih, Mène-Saffrané, Laurent, Gfeller, David, Asojo, Oluwatoyin A., and Schneiter, Roger

Abstract

Members of the CAP superfamily (cysteine-rich secretory proteins, antigen 5, and pathogenesis related 1 proteins), also known as SCP superfamily (sperm-coating proteins), have been implicated in many physiological processes, including immune defenses, venom toxicity, and sperm maturation. Their mode of action, however, remains poorly understood. Three proteins of the CAP superfamily, Pry1, 2, and 3 (pathogen related in yeast) are encoded in the S. cerevisiae genome. We have previously shown that Pry1 binds cholesterol in vitro and that Pry function is required for sterol secretion in yeast cells, indicating that members of this superfamily may generally bind sterols or related small hydrophobic compounds. On the other hand, tablysin-15, a CAP protein from the horsefly Tabanus yao, has been shown to bind leukotrienes and free fatty acids in vitro. Therefore, here we assessed whether the yeast Pry1 protein binds fatty acids. Computational modeling and site-directed mutagenesis indicated that the mode of fatty acid binding is conserved between tablysin-15 and Pry1. Pry1 bound fatty acids with micromolar affinity in vitro and its function was essential for fatty acid export in cells lacking the acyl-CoA synthetases Faa1 and Faa4. Fatty acid binding of Pry1 is independent of its capacity to bind sterols and the two sterol- and fatty acid-binding sites are non-overlapping. These results indicate that some CAP family members, such as Pry1, can bind different lipids, particularly sterols and fatty acids, at distinct binding sites, suggesting that the CAP domain may serve as a stable, secreted protein domain that can accommodate multiple ligand-binding sites.

Published
2017

37. Structure of SALO, a leishmaniasis vaccine candidate from the sand fly Lutzomyia longipalpis (Volume 11, Number 3)

Author

Asojo, Oluwatoyin A., Kelleher, Alan, and Liu, Zhuyun

Abstract

Background Immunity to the sand fly salivary protein SALO (Salivary Anticomplement of Lutzomyialongipalpis) protected hamsters against Leishmania infantum and L. braziliensis infection and, more recently, a vaccine combination of a genetically modified Leishmania with SALO conferred strong protection against L. donovani infection. Because of the importance of SALO as a potential component of a leishmaniasis vaccine, a plan to produce this recombinant protein for future scale manufacturing as well as knowledge of its structural characteristics are needed to move SALO forward for the clinical path. Methodology/Principal findings Recombinant SALO was expressed as a soluble secreted protein using Pichia pastoris, rSALO(P), with yields of 1g/L and >99% purity as assessed by SEC-MALS and SDS-PAGE. Unlike its native counterpart, rSALO(P) does not inhibit the classical pathway of complement; however, antibodies to rSALO(P) inhibit the anti-complement activity of sand fly salivary gland homogenate. Immunization with rSALO(P) produces a delayed type hypersensitivity response in C57BL/6 mice, suggesting rSALO(P) lacked anti-complement activity but retained its immunogenicity. The structure of rSALO(P) was solved by S-SAD at Cu-Kalpha to 1.94 Å and refined to Rfactor 17%. SALO is ~80% helical, has no appreciable structural similarities to any human protein, and has limited structural similarity in the C-terminus to members of insect odorant binding proteins. SALO has three predicted human CD4+ T cell epitopes on surface exposed helices.

Published
2017

41. Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: The crystal structure suggests two alternative mechanisms

Author

Nachon, Florian, Asojo, Oluwatoyin A., Borgstahl, Gloria E.O., Masson, Patrick, and Lockridge, Oksana

Subjects
Histidine -- Structure, Histidine -- Research, Cholinesterase inhibitors -- Research, Crystals -- Structure, Crystals -- Research, Biological sciences, Chemistry
Abstract

The crystal structures of human butyrylcholinesterase (hBChE) inhibited by the ophthalmic reagents echothiophate and diisopropylfluorophosphate are solved and refined to 2.1, 2.25, 2.2 angstrom resolution, respectively. The nonaged hBChE structure shows one water molecule interacting with Glu197 and the catalytic triad histidine (his 438), where the water molecule is positioned to promote aging by breaking either a C-O bond or a P-O bond.

Published
2005

45. Structure of SALO, a leishmaniasis vaccine candidate from the sand fly Lutzomyia longipalpis

Author

Asojo, Oluwatoyin A., primary, Kelleher, Alan, additional, Liu, Zhuyun, additional, Pollet, Jeroen, additional, Hudspeth, Elissa M., additional, Rezende, Wanderson C., additional, Groen, Mallory Jo, additional, Seid, Christopher A., additional, Abdeladhim, Maha, additional, Townsend, Shannon, additional, de Castro, Waldione, additional, Mendes-Sousa, Antonio, additional, Bartholomeu, Daniella Castanheira, additional, Fujiwara, Ricardo Toshio, additional, Bottazzi, Maria Elena, additional, Hotez, Peter J., additional, Zhan, Bin, additional, Oliveira, Fabiano, additional, Kamhawi, Shaden, additional, and Valenzuela, Jesus G., additional

Published
2017
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49. Expression and purification of an engineered, yeast-expressedLeishmania donovaninucleoside hydrolase with immunogenic properties

Author

Hudspeth, Elissa M., primary, Wang, Qian, additional, Seid, Christopher A., additional, Hammond, Molly, additional, Wei, Junfei, additional, Liu, Zhuyun, additional, Zhan, Bin, additional, Pollet, Jeroen, additional, Heffernan, Michael J., additional, McAtee, C Patrick, additional, Engler, David A., additional, Matsunami, Risë K., additional, Strych, Ulrich, additional, Asojo, Oluwatoyin A., additional, Hotez, Peter J., additional, and Bottazzi, Maria Elena, additional

Published
2016
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50. Crystal structure of chorismate mutase from <italic>Burkholderia thailandensis</italic>.

Author

Asojo, Oluwatoyin A., Dranow, David M., Serbzhinskiy, Dmitry, Subramanian, Sandhya, Staker, Bart, Edwards, Thomas E., and Myler, Peter J.

Subjects
*BURKHOLDERIA thailandensis, *CHORISMATE mutase
Abstract

Burkholderia thailandensis is often used as a model for more virulent members of this genus of proteobacteria that are highly antibiotic‐resistant and are potential agents of biological warfare that are infective by inhalation. As part of ongoing efforts to identify potential targets for the development of rational therapeutics, the structures of enzymes that are absent in humans, including that of chorismate mutase from B. thailandensis, have been determined by the Seattle Structural Genomics Center for Infectious Disease. The high‐resolution structure of chorismate mutase from B. thailandensis was determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQγ topology and shares conserved binding‐cavity residues with other chorismate mutases, including those with which it has no appreciable sequence identity. [ABSTRACT FROM AUTHOR]

Published
2018
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