LIVIVO - Search results -

Search results

Result 1 - 10 of total 130

Search options

Article ; Online: mRNA vaccines expressing malaria transmission-blocking antigens Pfs25 and Pfs230D1 induce a functional immune response.

Scaria, Puthupparampil V / Roth, Nicole / Schwendt, Kim / Muratova, Olga V / Alani, Nada / Lambert, Lynn E / Barnafo, Emma K / Rowe, Christopher G / Zaidi, Irfan U / Rausch, Kelly M / Narum, David L / Petsch, Benjamin / Duffy, Patrick E

NPJ vaccines

2024 Volume 9, Issue 1, Page(s) 9

Abstract: Malaria transmission-blocking vaccines (TBV) are designed to inhibit the sexual stage development of the parasite in the mosquito host and can play a significant role in achieving the goal of malaria elimination. Preclinical and clinical studies using ... ...

Abstract	Malaria transmission-blocking vaccines (TBV) are designed to inhibit the sexual stage development of the parasite in the mosquito host and can play a significant role in achieving the goal of malaria elimination. Preclinical and clinical studies using protein-protein conjugates of leading TBV antigens Pfs25 and Pfs230 domain 1 (Pfs230D1) have demonstrated the feasibility of TBV. Nevertheless, other promising vaccine platforms for TBV remain underexplored. The recent success of mRNA vaccines revealed the potential of this technology for infectious diseases. We explored the mRNA platform for TBV development. mRNA constructs of Pfs25 and Pfs230D1 variously incorporating signal peptides (SP), GPI anchor, and Trans Membrane (TM) domain were assessed in vitro for antigen expression, and selected constructs were evaluated in mice. Only mRNA constructs with GPI anchor or TM domain that resulted in high cell surface expression of the antigens yielded strong immune responses in mice. These mRNA constructs generated higher transmission-reducing functional activity versus the corresponding alum-adjuvanted protein-protein conjugates used as comparators. Pfs25 mRNA with GPI anchor or TM maintained >99% transmission reducing activity through 126 days, the duration of the study, demonstrating the potential of mRNA platform for TBV.
Language	English
Publishing date	2024-01-06
Publishing country	England
Document type	Journal Article
ISSN	2059-0105
ISSN (online)	2059-0105
DOI	10.1038/s41541-023-00783-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Host cell protein quantification of an optimized purification method by mass spectrometry.

Reiter, Karine / Suzuki, Motoshi / Olano, Lisa Renee / Narum, David L

Journal of pharmaceutical and biomedical analysis

2019 Volume 174, Page(s) 650–654

Abstract: Recombinant ExoProtein A (EPA), a detoxified form of Pseudomonas aeruginosa Exotoxin A, is used as a protein carrier in the vaccine field. A scaled manufacturing process, in which EPA was expressed in Escherichia coli, yielded a product that approached ... ...

Abstract	Recombinant ExoProtein A (EPA), a detoxified form of Pseudomonas aeruginosa Exotoxin A, is used as a protein carrier in the vaccine field. A scaled manufacturing process, in which EPA was expressed in Escherichia coli, yielded a product that approached or exceeded our upper limit of E. coli host cell protein (HCP) content per human dose. The purification process was redeveloped to reduce HCP levels in the bulk product and HCP content was evaluated by orthogonal methods. Using a platform specific immunoassay, the HCP level from the original purification method was 1,830 ppm (0.18% w/w) while the revised purification process yielded the HCP below the detection limits of the assay. With a 2D/LC-MS
MeSH term(s)	ADP Ribose Transferases/isolation & purification ; Algorithms ; Antibodies, Monoclonal/chemistry ; Bacterial Toxins/isolation & purification ; Chromatography, Liquid/methods ; Enzyme-Linked Immunosorbent Assay ; Escherichia coli/metabolism ; Exotoxins/isolation & purification ; False Positive Reactions ; Immunoblotting ; Proteolysis ; Recombinant Proteins/isolation & purification ; Reproducibility of Results ; Tandem Mass Spectrometry/methods ; Virulence Factors/isolation & purification ; Pseudomonas aeruginosa Exotoxin A
Chemical Substances	Antibodies, Monoclonal ; Bacterial Toxins ; Exotoxins ; Recombinant Proteins ; Virulence Factors ; ADP Ribose Transferases (EC 2.4.2.-)
Language	English
Publishing date	2019-06-28
Publishing country	England
Document type	Journal Article
ZDB-ID	604917-5
ISSN	1873-264X ; 0731-7085
ISSN (online)	1873-264X
ISSN	0731-7085
DOI	10.1016/j.jpba.2019.06.038
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1850: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Extending the range of Plasmodium falciparum transmission blocking antibodies

Simons, Lacy M. / Ferrer, Patricia / Gombakomba, Nita / Underwood, Knashka / Herrera, Raúl / Narum, David L. / Canepa, Gaspar / Acquah, Festus / Amoah, Linda / Duffy, Patrick E. / Barillas-Mury, Carolina / Long, Carole / Lee, Shwu-Maan / Locke, E. / Miura, Kazutoyo / Williamson, Kim C.

Vaccine.

2023

Abstract: Recent work demonstrating that asymptomatic carriers of P. falciparum parasites make up a large part of the infectious reservoir highlights the need for an effective malaria vaccine. Given the historical challenges of vaccine development, multiple ... ...

Abstract	Recent work demonstrating that asymptomatic carriers of P. falciparum parasites make up a large part of the infectious reservoir highlights the need for an effective malaria vaccine. Given the historical challenges of vaccine development, multiple parasite stages have been targeted, including the sexual stages required for transmission. Using flow cytometry to efficiently screen for P. falciparum gamete/zygote surface reactivity, we identified 82 antibodies that bound live P. falciparum gametes/zygotes. Ten antibodies had significant transmission-reducing activity (TRA) in a standard membrane feeding assay and were subcloned along with 9 nonTRA antibodies as comparators. After subcloning, only eight of the monoclonals obtained have significant TRA. These eight TRA mAbs do not recognize epitopes present in any of the current recombinant transmission-blocking vaccine candidates, Pfs230D1M, Pfs48/45.6C, Pf47 D2 and rPfs25. One TRA mAb immunoprecipitates two surface antigens, Pfs47 and Pfs230, that are expressed by both gametocytes and gametes/zygotes. These two proteins have not previously been reported to associate and the recognition of both by a single TRA mAb suggests the Pfs47/Pfs230 complex is a new vaccine target. In total, Pfs230 was the dominant target antigen, with five of the eight TRA mAbs and 8 of 11 nonTRA gamete/zygote surface reactive mAbs interacting with Pfs230. Of the three remaining TRA mAbs, two recognized non-reduced, parasite-produced Pfs25 and one bound non-reduced, parasite-produced Pfs48/45. None of the TRA mAbs bound protein on an immunoblot of reduced gamete/zygote extract and two TRA mAbs were immunoblot negative, indicating none of the new TRA epitopes are linear. The identification of eight new TRA mAbs that bind epitopes not included in any of the constructs currently under advancement as transmission-blocking vaccine candidates may provide new targets worthy of further study.
Keywords	Plasmodium falciparum ; epitopes ; flow cytometry ; gametocytes ; malaria vaccines ; parasites ; vaccine development ; zygote ; Malaria transmission ; Vaccines ; Monoclonal antibody screen ; Plasmodium falciparum gametes ; Mosquito membrane feed ; 6-cys ; ABTS ; BB ; BCIP ; BSA ; CCD ; cRPMI ; CSP ; Conc ; EB ; Ec ; EDTA ; ELISA ; EPA ; F6 ; FBS ; Gc ; Gm ; GPI ; HAT, hypoxanthine ; HI ; Inf ; Ippt ; mAbs ; Mem ; MPL-TDM ; MS/MS ; NAG ; NBT ; nr ; PBS ; PI ; r ; RBC ; RTS,S ; SDS ; SMFA ; TBS-T ; TRA ; TRA mAbs ; Tris-Cl
Language	English
Publishing place	Elsevier Ltd
Document type	Article ; Online
Note	Pre-press version
ZDB-ID	605674-x
ISSN	1873-2518 ; 0264-410X
ISSN (online)	1873-2518
ISSN	0264-410X
DOI	10.1016/j.vaccine.2023.04.042
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1930: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 458: Show issues

Order via subito

Details ▾

Article ; Online: Preclinical evaluations of Pfs25-EPA and Pfs230D1-EPA in AS01 for a vaccine to reduce malaria transmission.

Rausch, Kelly M / Barnafo, Emma K / Lambert, Lynn E / Muratova, Olga / Gorres, J Patrick / Anderson, Charles / Narum, David L / Wu, Yimin / Morrison, Robert D / Zaidi, Irfan / Duffy, Patrick E

iScience

2023 Volume 26, Issue 7, Page(s) 107192

Abstract: Malaria transmission-blocking vaccine candidates Pfs25-EPA and Pfs230D1-EPA target sexual stage development ... ...

Abstract	Malaria transmission-blocking vaccine candidates Pfs25-EPA and Pfs230D1-EPA target sexual stage development of
Language	English
Publishing date	2023-06-22
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2023.107192
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: A Plasmodium falciparum RING Finger E3 Ubiquitin Ligase Modifies the Roles of PfMDR1 and PfCRT in Parasite Drug Responses.

Singh, Brajesh K / Zhang, Cui / Wu, Jian / Peng, Yu-Chih / He, Xiao / Tumas, Keyla C / Sá, Juliana M / Lane, Kristin D / Eastman, Richard T / Narum, David L / Wellems, Thomas E / Su, Xin-Zhuan

Antimicrobial agents and chemotherapy

2023 Volume 67, Issue 2, Page(s) e0082122

Abstract: Protein ubiquitination is an important posttranslational regulation mechanism that ... ...

Abstract	Protein ubiquitination is an important posttranslational regulation mechanism that mediates
MeSH term(s)	Humans ; Antimalarials/pharmacology ; Chloroquine/pharmacology ; Drug Resistance/genetics ; Malaria, Falciparum/drug therapy ; Membrane Transport Proteins/genetics ; Multidrug Resistance-Associated Proteins/genetics ; Plasmodium falciparum/drug effects ; Plasmodium falciparum/genetics ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Antimalarials ; Chloroquine (886U3H6UFF) ; Membrane Transport Proteins ; Multidrug Resistance-Associated Proteins ; Protozoan Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2023-01-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/aac.00821-22
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 809: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Einzelsignatur: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A human antibody epitope map of Pfs230D1 derived from analysis of individuals vaccinated with a malaria transmission-blocking vaccine.

Tang, Wai Kwan / Coelho, Camila H / Miura, Kazutoyo / Nguemwo Tentokam, Bergeline C / Salinas, Nichole D / Narum, David L / Healy, Sara A / Sagara, Issaka / Long, Carole A / Duffy, Patrick E / Tolia, Niraj H

Immunity

2023 Volume 56, Issue 2, Page(s) 433–443.e5

Abstract: Pfs230 domain 1 (Pfs230D1) is an advanced malaria transmission-blocking vaccine antigen demonstrating high functional activity in clinical trials. However, the structural and functional correlates of transmission-blocking activity are not defined. Here, ... ...

Abstract	Pfs230 domain 1 (Pfs230D1) is an advanced malaria transmission-blocking vaccine antigen demonstrating high functional activity in clinical trials. However, the structural and functional correlates of transmission-blocking activity are not defined. Here, we characterized a panel of human monoclonal antibodies (hmAbs) elicited in vaccinees immunized with Pfs230D1. These hmAbs exhibited diverse transmission-reducing activity, yet all bound to Pfs230D1 with nanomolar affinity. We compiled epitope-binning data for seventeen hmAbs and structures of nine hmAbs complexes to construct a high-resolution epitope map and revealed that potent transmission-reducing hmAbs bound to one face of Pfs230D1, while non-potent hmAbs bound to the opposing side. The structure of Pfs230D1D2 revealed that non-potent transmission-reducing epitopes were occluded by the second domain. The hmAb epitope map delineated binary hmAb combinations that synergized for extremely high-potency, transmission-reducing activity. This work provides a high-resolution guide for structure-based design of enhanced immunogens and informs diagnostics that measure the transmission-reducing response.
MeSH term(s)	Humans ; Epitopes ; Malaria Vaccines ; Antibodies, Neutralizing ; Antigens ; Antibodies, Viral
Chemical Substances	Epitopes ; Malaria Vaccines ; Antibodies, Neutralizing ; Antigens ; Antibodies, Viral
Language	English
Publishing date	2023-02-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1217235-2
ISSN	1097-4180 ; 1074-7613
ISSN (online)	1097-4180
ISSN	1074-7613
DOI	10.1016/j.immuni.2023.01.012
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 4227: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 69: Show issues

Order via subito

Details ▾

Article ; Online: Immunological characterization of a VIR protein family member (VIR-14) in Plasmodium vivax-infected subjects from different epidemiological regions in Africa and South America.

Fantin, Raianna F / Coelho, Camila H / Berhe, Anne D / Magalhães, Luisa M D / Pereira, Dhélio B / Salinas, Nichole D / Tolia, Niraj H / Amaratunga, Chanaki / Suon, Seila / Sagara, Issaka / Narum, David L / Fujiwara, Ricardo T / Abejon, Claudia / Campos-Neto, Antonio / Duffy, Patrick E / Bueno, Lilian L

PLoS neglected tropical diseases

2023 Volume 17, Issue 4, Page(s) e0011229

Abstract: Plasmodium vivax is a major challenge for malaria control due to its wide geographic distribution, high frequency of submicroscopic infections, and ability to induce relapses due to the latent forms present in the liver (hypnozoites). Deepening our ... ...

Abstract	Plasmodium vivax is a major challenge for malaria control due to its wide geographic distribution, high frequency of submicroscopic infections, and ability to induce relapses due to the latent forms present in the liver (hypnozoites). Deepening our knowledge of parasite biology and its molecular components is key to develop new tools for malaria control and elimination. This study aims to investigate and characterize a P. vivax protein (PvVir14) for its role in parasite biology and its interactions with the immune system. We collected sera or plasma from P.vivax-infected subjects in Brazil (n = 121) and Cambodia (n = 55), and from P. falciparum-infected subjects in Mali (n = 28), to assess antibody recognition of PvVir14. Circulating antibodies against PvVir14 appeared in 61% and 34.5% of subjects from Brazil and Cambodia, respectively, versus none (0%) of the P. falciparum-infected subjects from Mali who have no exposure to P. vivax. IgG1 and IgG3 most frequently contributed to anti-PvVir14 responses. PvVir14 antibody levels correlated with those against other well-characterized sporozoite/liver (PvCSP) and blood stage (PvDBP-RII) antigens, which were recognized by 7.6% and 42% of Brazilians, respectively. Concerning the cellular immune profiling of Brazilian subjects, PvVir14 seroreactive individuals displayed significantly higher levels of circulating atypical (CD21- CD27-) B cells, raising the possibility that atypical B cells may be contribute to the PvVir14 antibody response. When analyzed at a single-cell level, the B cell receptor gene hIGHV3-23 was only seen in subjects with active P.vivax infection where it comprised 20% of V gene usage. Among T cells, CD4+ and CD8+ levels differed (lower and higher, respectively) between subjects with versus without antibodies to PvVir14, while NKT cell levels were higher in those without antibodies. Specific B cell subsets, anti-PvVir14 circulating antibodies, and NKT cell levels declined after treatment of P. vivax. This study provides the immunological characterization of PvVir14, a unique P. vivax protein, and possible association with acute host's immune responses, providing new information of specific host-parasite interaction. Trial registration: TrialClinicalTrials.gov Identifier: NCT00663546 & ClinicalTrials.gov NCT02334462.
MeSH term(s)	Humans ; Plasmodium vivax/genetics ; Protozoan Proteins/genetics ; Antigens, Protozoan ; Plasmodium falciparum ; Antibodies, Protozoan ; Malaria, Vivax/parasitology ; Malaria, Falciparum/epidemiology ; Brazil/epidemiology ; Family ; Immunoglobulin G ; Mali/epidemiology
Chemical Substances	Protozoan Proteins ; Antigens, Protozoan ; Antibodies, Protozoan ; Immunoglobulin G
Language	English
Publishing date	2023-04-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Intramural
ZDB-ID	2429704-5
ISSN	1935-2735 ; 1935-2735
ISSN (online)	1935-2735
ISSN	1935-2735
DOI	10.1371/journal.pntd.0011229
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: RTS,S/AS02A Malaria Vaccine-Induced IgG Responses Equally Recognize Native-Like Fucosylated and Nonfucosylated Plasmodium falciparum Circumsporozoite Proteins.

Jairoce, Chenjerai / Macià, Dídac / Torres-Yaguana, Jorge P / Mayer, Leonie / Vidal, Marta / Santano, Rebeca / Hurtado-Guerrero, Ramón / Reiter, Karine / Narum, David L / Lopez-Gutierrez, Borja / Hamerly, Timothy / Sacarlal, Jahit / Aguilar, Ruth / Dinglasan, Rhoel R / Moncunill, Gemma / Izquierdo, Luis / Dobaño, Carlota

The Journal of infectious diseases

2023 Volume 229, Issue 3, Page(s) 795–799

Abstract: The RTS,S/AS02A malaria vaccine is based on the Plasmodium falciparum circumsporozoite protein (PfCSP), which is O-fucosylated on the sporozoite surface. We determined whether RTS,S/AS02A-induced immunoglobulin G (IgG) antibodies recognize vaccine-like ... ...

Abstract	The RTS,S/AS02A malaria vaccine is based on the Plasmodium falciparum circumsporozoite protein (PfCSP), which is O-fucosylated on the sporozoite surface. We determined whether RTS,S/AS02A-induced immunoglobulin G (IgG) antibodies recognize vaccine-like nonfucosylated PfCSP better than native-like fucosylated PfCSP. Similar to previous vaccine trials, RTS,S/AS02A vaccination induced high anti-PfCSP IgG levels associated with malaria protection. IgG recognition of nonfucosylated and fucosylated PfCSP was equivalent, suggesting that PfCSP fucosylation does not affect antibody recognition. Clinical Trials Registration. NCT00197041.
MeSH term(s)	Humans ; Malaria Vaccines ; Plasmodium falciparum ; Malaria, Falciparum/prevention & control ; Immunoglobulin G ; Antibodies, Protozoan ; Protozoan Proteins
Chemical Substances	Malaria Vaccines ; Immunoglobulin G ; Antibodies, Protozoan ; Protozoan Proteins
Language	English
Publishing date	2023-10-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiad471
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Uh II Zs.50: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MO 445: Show issues

Order via subito

Details ▾

Article ; Online: Extending the range of Plasmodium falciparum transmission blocking antibodies.

Simons, Lacy M / Ferrer, Patricia / Gombakomba, Nita / Underwood, Knashka / Herrera, Raul / Narum, David L / Canepa, Gaspar / Acquah, Festus / Amoah, Linda / Duffy, Patrick E / Barillas-Mury, Carolina / Long, Carole / Lee, Shwu-Maan / Locke, Emily / Miura, Kazutoyo / Williamson, Kim C

Vaccine

2023 Volume 41, Issue 21, Page(s) 3367–3379

Abstract	Recent work demonstrating that asymptomatic carriers of P. falciparum parasites make up a large part of the infectious reservoir highlights the need for an effective malaria vaccine. Given the historical challenges of vaccine development, multiple parasite stages have been targeted, including the sexual stages required for transmission. Using flow cytometry to efficiently screen for P. falciparum gamete/zygote surface reactivity, we identified 82 antibodies that bound live P. falciparum gametes/zygotes. Ten antibodies had significant transmission-reducing activity (TRA) in a standard membrane feeding assay and were subcloned along with 9 nonTRA antibodies as comparators. After subcloning, only eight of the monoclonals obtained have significant TRA. These eight TRA mAbs do not recognize epitopes present in any of the current recombinant transmission-blocking vaccine candidates, Pfs230D1M, Pfs48/45.6C, Pf47 D2 and rPfs25. One TRA mAb immunoprecipitates two surface antigens, Pfs47 and Pfs230, that are expressed by both gametocytes and gametes/zygotes. These two proteins have not previously been reported to associate and the recognition of both by a single TRA mAb suggests the Pfs47/Pfs230 complex is a new vaccine target. In total, Pfs230 was the dominant target antigen, with five of the eight TRA mAbs and 8 of 11 nonTRA gamete/zygote surface reactive mAbs interacting with Pfs230. Of the three remaining TRA mAbs, two recognized non-reduced, parasite-produced Pfs25 and one bound non-reduced, parasite-produced Pfs48/45. None of the TRA mAbs bound protein on an immunoblot of reduced gamete/zygote extract and two TRA mAbs were immunoblot negative, indicating none of the new TRA epitopes are linear. The identification of eight new TRA mAbs that bind epitopes not included in any of the constructs currently under advancement as transmission-blocking vaccine candidates may provide new targets worthy of further study.
MeSH term(s)	Humans ; Plasmodium falciparum ; Antibodies, Blocking ; Malaria, Falciparum ; Epitopes ; Antibodies, Protozoan ; Antibodies, Monoclonal ; Malaria Vaccines ; Protozoan Proteins ; Antigens, Protozoan
Chemical Substances	Antibodies, Blocking ; Epitopes ; Antibodies, Protozoan ; Antibodies, Monoclonal ; Malaria Vaccines ; Protozoan Proteins ; Antigens, Protozoan
Language	English
Publishing date	2023-04-24
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Intramural
ZDB-ID	605674-x
ISSN	1873-2518 ; 0264-410X
ISSN (online)	1873-2518
ISSN	0264-410X
DOI	10.1016/j.vaccine.2023.04.042
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1930: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 458: Show issues

Order via subito

Details ▾

Article ; Online: Structural and immunological differences in Plasmodium falciparum sexual stage transmission-blocking vaccines comprised of Pfs25-EPA nanoparticles.

NPJ vaccines

2023 Volume 8, Issue 1, Page(s) 56

Abstract: Development of a malaria vaccine that blocks transmission of different parasite stages to humans and mosquitoes is considered critical for elimination efforts. A vaccine using Pfs25, a protein on the surface of zygotes and ookinetes, is under ... ...

Abstract	Development of a malaria vaccine that blocks transmission of different parasite stages to humans and mosquitoes is considered critical for elimination efforts. A vaccine using Pfs25, a protein on the surface of zygotes and ookinetes, is under investigation as a transmission-blocking vaccine (TBV) that would interrupt parasite passage from mosquitoes to humans. The most extensively studied Pfs25 TBVs use Pichia pastoris-produced recombinant forms of Pfs25, chemically conjugated to a recombinant carrier protein, ExoProtein A (EPA). The recombinant form of Pfs25 first used in humans was identified as Pfs25H, which contained a total of 14 heterologous amino acid residues located at the amino- and carboxyl-termini including a His6 affinity tag. A second recombinant Pfs25, identified as Pfs25M, was produced to remove the heterologous amino acid residues and conjugated to EPA (Pfs25M-EPA). Here, monomeric Pfs25M was characterized biochemically and biophysically for identity, purity, and integrity including protein structure to assess its comparability with Pfs25H. Although the biological activities of Pfs25H and Pfs25M, whether generated by monomeric forms or conjugated nanoparticles, appeared similar, fine-mapping studies with two transmission-blocking monoclonal antibodies detected structural and immunological differences. In addition, evaluation of antisera generated against conjugated Pfs25H or Pfs25M nanoparticles in nonhuman primates identified polyclonal IgG that recognized these structural differences.
Language	English
Publishing date	2023-04-15
Publishing country	England
Document type	Journal Article
ISSN	2059-0105
ISSN (online)	2059-0105
DOI	10.1038/s41541-023-00655-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED