About: Process Characterization and Biophysical Analysis for a Yeast-Expressed Phlebotomus papatasi Salivary Protein (PpSP15) as a Leishmania Vaccine Candidate

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About: Process Characterization and Biophysical Analysis for a Yeast-Expressed Phlebotomus papatasi Salivary Protein (PpSP15) as a Leishmania Vaccine Candidate Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Process Characterization and Biophysical Analysis for a Yeast-Expressed Phlebotomus papatasi Salivary Protein (PpSP15) as a Leishmania Vaccine Candidate
Creator	Chen, Wen-Hsiang Strych, Ulrich Liu, Zhuyun Hotez, Peter Bottazzi, Maria Peak Nyon, Mun Biter, Amadeo Kundu, Rakhi Poongavanam, Mohan
Source	Elsevier; Medline; PMC
abstract	Abstract Cutaneous leishmaniasis is a neglected tropical disease caused by the parasite Leishmania and transmitted by sandflies. It has become a major health problem in many tropical and subtropical countries, especially in regions of conflict and political instability. Currently, there are only limited drug treatments and no available licensed vaccine; thus, the need for more therapeutic interventions remains urgent. Previously, a DNA vaccine encoding a 15 kDa sandfly (Phlebotomus papatasi) salivary protein (PpSP15) and recombinant nonpathogenic Leishmania tarentolae secreting PpSP15 have been shown to induce protective immunity against Leishmania major in mice, demonstrating that PpSP15 is a promising vaccine candidate. In this study, we developed a fermentation process in yeast with a yield of ~1g PpSP15/L and a scalable purification process consisting of only 2 chromatographic purification steps with high binding capacity for PpSP15, suggesting that PpSP15 can be produced economically. The biophysical/biochemical analysis of the purified PpSP15 indicated that the protein was of high purity (>97%) and conformationally stable between pH 4.4 and 9.0. More importantly, the recombinant protein had a defined structure similar to that of the related PdSP15 from Phlebotomus duboscqi, implying the suitability of the yeast expression system for producing a correctly folded PpSP15.
has issue date	2020-02-15(xsd:dateTime)
bibo:doi	10.1016/j.xphs.2020.02.004
bibo:pmid	32070701
has license	els-covid
sha1sum (hex)	7c10988e4f107c4fa8bc2ea3dae8df800de06ce9
schema:url	https://doi.org/10.1016/j.xphs.2020.02.004
resource representing a document's title	Process Characterization and Biophysical Analysis for a Yeast-Expressed Phlebotomus papatasi Salivary Protein (PpSP15) as a Leishmania Vaccine Candidate
has PubMed Central identifier	PMC7125844
has PubMed identifier	32070701
schema:publication	J Pharm Sci
resource representing a document's body	covid:7c10988e4f107c4fa8bc2ea3dae8df800de06ce9#body_text
is schema:about of	named entity 'ANALYSIS' named entity 'biophysical' named entity 'licensed' named entity 'high' named entity 'expression system' named entity 'Characterization' named entity 'PURIFICATION' named entity 'TROPICAL' named entity 'PREVIOUSLY' named entity 'SANDFLY' named entity 'VACCINE CANDIDATE' named entity 'NEGLECTED' named entity 'HEALTH PROBLEM' named entity 'PARASITE' named entity 'PRODUCING' named entity 'REGIONS' named entity 'TROPICAL DISEASE' named entity 'FERMENTATION PROCESS' named entity 'STUDY' named entity 'EXPRESSION SYSTEM' named entity 'INDICATED' named entity 'STRUCTURE' named entity 'LEISHMANIA TARENTOLAE' named entity 'LEISHMANIA' named entity 'TREATMENTS' named entity 'ENCODING' named entity 'CHARACTERIZATION' named entity 'LICENSED VACCINE' named entity 'YIELD' named entity 'CAUSED BY' named entity 'AVAILABLE' named entity 'YEAST' named entity 'SALIVARY PROTEIN' named entity 'FOLDED' named entity 'BINDING CAPACITY' named entity 'DNA VACCINE' named entity 'PROCESS' named entity 'PROCESS' named entity 'LEISHMANIA VACCINE' named entity 'PHLEBOTOMUS PAPATASI' named entity 'PROTECTIVE IMMUNITY' named entity 'PURIFIED' named entity 'SALIVARY PROTEIN' named entity 'ANALYSIS' named entity 'URGENT' named entity 'DRUG' named entity 'INDUCE' named entity 'VACCINE CANDIDATE' named entity 'TRANSMITTED BY' named entity 'RECOMBINANT PROTEIN' named entity 'SANDFLIES' named entity 'CUTANEOUS LEISHMANIASIS' named entity '4.4' named entity 'SUBTROPICAL' named entity 'SECRETING' named entity 'INSTABILITY' named entity 'HAVE' named entity 'BIOPHYSICAL' named entity 'A DNA' named entity 'PURITY' named entity 'ECONOMICALLY' named entity 'CONFLICT' named entity 'MICE' named entity 'PHLEBOTOMUS DUBOSCQI' named entity 'COUNTRIES' named entity 'CURRENTLY' named entity 'THERAPEUTIC INTERVENTIONS' named entity 'PROTEIN ' named entity 'SIMILAR' named entity 'KDA' named entity 'DEFINED' named entity 'A MAJOR' named entity 'HIGH'

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