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Book ; Thesis: Klonierung und Charakterisisierung eines Gens (GPI-1) der Biosynthese des GPI-Toxins des Malariaerregers Plasmodium falciparum

Shams-Eldin, Hosam M. H.

(Wissenschaft in Dissertationen ; 656)

2001

Author's details	von Hosam M. H. Shams-Eldin
Series title	Wissenschaft in Dissertationen ; 656
Collection
Keywords	Plasmodium falciparum ; Glykosylphosphatidylinosit-Anker ; Genklonierung
Subject	Klonierung ; Gen-Isolierung ; Molekulare Klonierung ; Kloniertes Gen ; GPI-Anker ; Glycosylphosphatidylinositol-Membrananker
Language	German
Size	102 S., Ill., graph. Darst., 21 cm
Publisher	Görich und Weiershäuser
Publishing place	Marburg
Publishing country	Germany
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Gießen, Univ., Diss., 2001
HBZ-ID	HT013442681
ISBN	3-89703-490-5 ; 978-3-89703-490-7
Database	Catalogue ZB MED Medicine, Health

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Article: Comparative Study of a Novel Lateral Flow Rapid Test with Conventional Serological Test Systems for the Diagnosis of Canine Leishmaniosis in Croatia and Brazil.

Mahdavi, Rouzbeh / Martinkovic, Franjo / Shams-Eldin, Hosam / Pereira, Ingrid E / Reis, Alexandre B / Latz, Andreas / Heinz, Daniela / Aira, Cristina / Fresco-Taboada, Alba / Abass, Elfadil / Romero-Olmedo, Jelena / Teixeira, Henrique C / Steinhoff, Ulrich

Pathogens (Basel, Switzerland)

2024 Volume 13, Issue 2

Abstract: Control of canine infections ... ...

Abstract	Control of canine infections with
Language	English
Publishing date	2024-01-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2695572-6
ISSN	2076-0817
ISSN	2076-0817
DOI	10.3390/pathogens13020109
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Article ; Online: FT-GPI, a highly sensitive and accurate predictor of GPI-anchored proteins, reveals the composition and evolution of the GPI proteome in Plasmodium species.

Sauer, Lena M / Canovas, Rodrigo / Roche, Daniel / Shams-Eldin, Hosam / Ravel, Patrice / Colinge, Jacques / Schwarz, Ralph T / Ben Mamoun, Choukri / Rivals, Eric / Cornillot, Emmanuel

Malaria journal

2023 Volume 22, Issue 1, Page(s) 27

Abstract: Background: Protozoan parasites are known to attach specific and diverse group of proteins to their plasma membrane via a GPI anchor. In malaria parasites, GPI-anchored proteins (GPI-APs) have been shown to play an important role in host-pathogen ... ...

Abstract	Background: Protozoan parasites are known to attach specific and diverse group of proteins to their plasma membrane via a GPI anchor. In malaria parasites, GPI-anchored proteins (GPI-APs) have been shown to play an important role in host-pathogen interactions and a key function in host cell invasion and immune evasion. Because of their immunogenic properties, some of these proteins have been considered as malaria vaccine candidates. However, identification of all possible GPI-APs encoded by these parasites remains challenging due to their sequence diversity and limitations of the tools used for their characterization. Methods: The FT-GPI software was developed to detect GPI-APs based on the presence of a hydrophobic helix at both ends of the premature peptide. FT-GPI was implemented in C ++and applied to study the GPI-proteome of 46 isolates of the order Haemosporida. Using the GPI proteome of Plasmodium falciparum strain 3D7 and Plasmodium vivax strain Sal-1, a heuristic method was defined to select the most sensitive and specific FT-GPI software parameters. Results: FT-GPI enabled revision of the GPI-proteome of P. falciparum and P. vivax, including the identification of novel GPI-APs. Orthology- and synteny-based analyses showed that 19 of the 37 GPI-APs found in the order Haemosporida are conserved among Plasmodium species. Our analyses suggest that gene duplication and deletion events may have contributed significantly to the evolution of the GPI proteome, and its composition correlates with speciation. Conclusion: FT-GPI-based prediction is a useful tool for mining GPI-APs and gaining further insights into their evolution and sequence diversity. This resource may also help identify new protein candidates for the development of vaccines for malaria and other parasitic diseases.
MeSH term(s)	GPI-Linked Proteins/genetics ; Plasmodium falciparum/genetics ; Plasmodium vivax/genetics ; Proteome/analysis ; Protozoan Proteins/genetics
Chemical Substances	GPI-Linked Proteins ; Proteome ; Protozoan Proteins
Language	English
Publishing date	2023-01-25
Publishing country	England
Document type	Journal Article
ZDB-ID	2091229-8
ISSN	1475-2875 ; 1475-2875
ISSN (online)	1475-2875
ISSN	1475-2875
DOI	10.1186/s12936-022-04430-0
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Article ; Online: Development of a Novel Enzyme-Linked Immunosorbent Assay and Lateral Flow Test System for Improved Serodiagnosis of Visceral Leishmaniasis in Different Areas of Endemicity.

Mahdavi, Rouzbeh / Shams-Eldin, Hosam / Witt, Sandra / Latz, Andreas / Heinz, Daniela / Fresco-Taboada, Alba / Aira, Cristina / Hübner, Marc P / Sukyte, Dalia / Visekruna, Alexander / Teixeira, Henrique C / Abass, Elfadil / Steinhoff, Ulrich

Microbiology spectrum

2023 Volume 11, Issue 3, Page(s) e0433822

Abstract: Visceral leishmaniasis (VL) is caused by protozoan parasites of the Leishmania donovani complex and is one of the most prominent vector-borne infectious diseases with epidemic and mortality potential if not correctly diagnosed and treated. East African ... ...

Abstract	Visceral leishmaniasis (VL) is caused by protozoan parasites of the Leishmania donovani complex and is one of the most prominent vector-borne infectious diseases with epidemic and mortality potential if not correctly diagnosed and treated. East African countries suffer from a very high incidence of VL, and although several diagnostic tests are available for VL, diagnosis continues to represent a big challenge in these countries due to the lack of sensitivity and specificity of current serological tools. Based on bioinformatic analysis, a new recombinant kinesin antigen from Leishmania infantum (rKLi8.3) was developed. The diagnostic performance of rKLi8.3 was evaluated by enzyme-linked immunosorbent assay (ELISA) and lateral flow test (LFT) on a panel of sera from Sudanese, Indian, and South American patients diagnosed with VL or other diseases, including tuberculosis, malaria, and trypanosomiasis. The diagnostic accuracy of rKLi8.3 was compared with rK39 and rKLO8 antigens. The VL-specific sensitivity of rK39, rKLO8, and rKLi8.3 ranged from 91.2% over 92.4% to 97.1% and specificity ranged from 93.6% over 97.6% to 99.2%, respectively. In India, all tests showed a comparable specificity of 90.9%, while the sensitivity ranged from 94.7% to 100% (rKLi8.3). In contrast to commercial serodiagnostic tests, rKLi8.3-based ELISA and LFT showed improved sensitivity and no cross-reactivity with other parasitic diseases. Thus, rKLi8.3-based ELISA and LFT offer improved VL serodiagnostic efficiency in East Africa and other areas of endemicity.
MeSH term(s)	Humans ; Leishmaniasis, Visceral/diagnosis ; Leishmaniasis, Visceral/epidemiology ; Leishmaniasis, Visceral/parasitology ; Antigens, Protozoan ; Protozoan Proteins ; Kinesins ; Serologic Tests ; Enzyme-Linked Immunosorbent Assay
Chemical Substances	Antigens, Protozoan ; Protozoan Proteins ; Kinesins (EC 3.6.4.4)
Language	English
Publishing date	2023-04-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2807133-5
ISSN	2165-0497 ; 2165-0497
ISSN (online)	2165-0497
ISSN	2165-0497
DOI	10.1128/spectrum.04338-22
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Article ; Online: AglH, a thermophilic UDP-N-acetylglucosamine-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase initiating protein N-glycosylation pathway in Sulfolobus acidocaldarius, is capable of complementing the eukaryal Alg7.

Meyer, Benjamin H / Shams-Eldin, Hosam / Albers, Sonja-Verena

Extremophiles : life under extreme conditions

2016 Volume 21, Issue 1, Page(s) 121–134

Abstract: AglH, a predicted UDP-GlcNAc-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase, is initiating the protein N-glycosylation pathway in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. AglH successfully replaced the endogenous GlcNAc-1- ...

Abstract	AglH, a predicted UDP-GlcNAc-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase, is initiating the protein N-glycosylation pathway in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. AglH successfully replaced the endogenous GlcNAc-1-phosphotransferase activity of Alg7 in a conditional lethal Saccharomyces cerevisiae strain, in which the first step of the eukaryal protein N-glycosylation process was repressed. This study is one of the few examples of cross-domain complementation demonstrating a conserved polyprenyl phosphate transferase reaction within the eukaryal and archaeal domain like it was demonstrated for Methanococcus voltae (Shams-Eldin et al. 2008). The topology prediction and the alignment of the AglH membrane protein with GlcNAc-1-phosphotransferases from the three domains of life show significant conservation of amino acids within the different proposed cytoplasmic loops. Alanine mutations of selected conserved amino acids in the putative cytoplasmic loops II (D
MeSH term(s)	Archaeal Proteins/chemistry ; Archaeal Proteins/genetics ; Archaeal Proteins/metabolism ; Conserved Sequence ; Genetic Complementation Test ; Phosphotransferases (Phosphate Group Acceptor)/genetics ; Protein Domains ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Sulfolobus acidocaldarius/enzymology ; Sulfolobus acidocaldarius/genetics ; Transferases (Other Substituted Phosphate Groups)/chemistry ; Transferases (Other Substituted Phosphate Groups)/genetics ; Transferases (Other Substituted Phosphate Groups)/metabolism
Chemical Substances	Archaeal Proteins ; Alg7 protein, S cerevisiae (EC 2.7.4.-) ; Phosphotransferases (Phosphate Group Acceptor) (EC 2.7.4.-) ; Transferases (Other Substituted Phosphate Groups) (EC 2.7.8.-) ; UDPacetylglucosamine-dolichyl-phosphate acetylglucosamine-1-phosphate transferase (EC 2.7.8.15)
Language	English
Publishing date	2016-11-07
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1481278-2
ISSN	1433-4909 ; 1431-0651
ISSN (online)	1433-4909
ISSN	1431-0651
DOI	10.1007/s00792-016-0890-2
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Article: Protective CD8+ T Cell Response Induced by Modified Vaccinia Virus Ankara Delivering Ebola Virus Nucleoprotein.

Kupke, Alexandra / Volz, Asisa / Dietzel, Erik / Freudenstein, Astrid / Schmidt, Jörg / Shams-Eldin, Hosam / Jany, Sylvia / Sauerhering, Lucie / Krähling, Verena / Gellhorn Serra, Michelle / Herden, Christiane / Eickmann, Markus / Becker, Stephan / Sutter, Gerd

Vaccines

2022 Volume 10, Issue 4

Abstract: The urgent need for vaccines against Ebola virus (EBOV) was underscored by the large outbreak in West Africa (2014-2016). Since then, several promising vaccine candidates have been tested in pre-clinical and clinical studies. As a result, two vaccines ... ...

Abstract	The urgent need for vaccines against Ebola virus (EBOV) was underscored by the large outbreak in West Africa (2014-2016). Since then, several promising vaccine candidates have been tested in pre-clinical and clinical studies. As a result, two vaccines were approved for human use in 2019/2020, of which one includes a heterologous adenovirus/Modified Vaccinia virus Ankara (MVA) prime-boost regimen. Here, we tested new vaccine candidates based on the recombinant MVA vector, encoding the EBOV nucleoprotein (MVA-EBOV-NP) or glycoprotein (MVA-EBOV-GP) for their efficacy after homologous prime-boost immunization in mice. Our aim was to investigate the role of each antigen in terms of efficacy and correlates of protection. Sera of mice vaccinated with MVA-EBOV-GP were virus-neutralizing and MVA-EBOV-NP immunization readily elicited interferon-γ-producing NP-specific CD8+ T cells. While mock-vaccinated mice succumbed to EBOV infection, all vaccinated mice survived and showed drastically decreased viral loads in sera and organs. In addition, MVA-EBOV-NP vaccinated mice became susceptible to lethal EBOV infection after depletion of CD8+ T cells prior to challenge. This study highlights the potential of MVA-based vaccines to elicit humoral immune responses as well as a strong and protective CD8+ T cell response and contributes to understanding the possible underlying mechanisms.
Language	English
Publishing date	2022-03-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines10040533
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Article ; Online: Selected commensals educate the intestinal vascular and immune system for immunocompetence.

Microbiome

2022 Volume 10, Issue 1, Page(s) 158

Abstract: Background: The intestinal microbiota fundamentally guides the development of a normal intestinal physiology, the education, and functioning of the mucosal immune system. The Citrobacter rodentium-carrier model in germ-free (GF) mice is suitable to ... ...

Abstract	Background: The intestinal microbiota fundamentally guides the development of a normal intestinal physiology, the education, and functioning of the mucosal immune system. The Citrobacter rodentium-carrier model in germ-free (GF) mice is suitable to study the influence of selected microbes on an otherwise blunted immune response in the absence of intestinal commensals. Results: Here, we describe that colonization of adult carrier mice with 14 selected commensal microbes (OMM Conclusions: Consortium modeling revealed that the addition of two facultative anaerobes to the OMM
MeSH term(s)	Animals ; Citrobacter rodentium/physiology ; Immune System ; Immunocompetence ; Intestinal Mucosa ; Intestines ; Mice
Language	English
Publishing date	2022-09-28
Publishing country	England
Document type	Journal Article ; Video-Audio Media ; Research Support, Non-U.S. Gov't
ZDB-ID	2697425-3
ISSN	2049-2618 ; 2049-2618
ISSN (online)	2049-2618
ISSN	2049-2618
DOI	10.1186/s40168-022-01353-5
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Article ; Online: Identification of O-GlcNAcylated proteins in Plasmodium falciparum.

Kupferschmid, Mattis / Aquino-Gil, Moyira Osny / Shams-Eldin, Hosam / Schmidt, Jörg / Yamakawa, Nao / Krzewinski, Frédéric / Schwarz, Ralph T / Lefebvre, Tony

Malaria journal

2017 Volume 16, Issue 1, Page(s) 485

Abstract: Background: Post-translational modifications (PTMs) constitute a huge group of chemical modifications increasing the complexity of the proteomes of living beings. PTMs have been discussed as potential anti-malarial drug targets due to their involvement ... ...

Abstract	Background: Post-translational modifications (PTMs) constitute a huge group of chemical modifications increasing the complexity of the proteomes of living beings. PTMs have been discussed as potential anti-malarial drug targets due to their involvement in many cell processes. O-GlcNAcylation is a widespread PTM found in different organisms including Plasmodium falciparum. The aim of this study was to identify O-GlcNAcylated proteins of P. falciparum, to learn more about the modification process and to understand its eventual functions in the Apicomplexans. Methods: The P. falciparum strain 3D7 was amplified in erythrocytes and purified. The proteome was checked for O-GlcNAcylation using different methods. The level of UDP-GlcNAc, the donor of the sugar moiety for O-GlcNAcylation processes, was measured using high-pH anion exchange chromatography. O-GlcNAcylated proteins were enriched and purified utilizing either click chemistry labelling or adsorption on succinyl-wheat germ agglutinin beads. Proteins were then identified by mass-spectrometry (nano-LC MS/MS). Results: While low when compared to MRC5 control cells, P. falciparum disposes of its own pool of UDP-GlcNAc. By using proteomics methods, 13 O-GlcNAcylated proteins were unambiguously identified (11 by click-chemistry and 6 by sWGA-beads enrichment; 4 being identified by the 2 approaches) in late trophozoites. These proteins are all part of pathways, functions and structures important for the parasite survival. By probing clicked-proteins with specific antibodies, Hsp70 and α-tubulin were identified as P. falciparum O-GlcNAc-bearing proteins. Conclusions: This study is the first report on the identity of P. falciparum O-GlcNAcylated proteins. While the parasite O-GlcNAcome seems close to those of other species, the structural differences exhibited by the proteomes provides a glimpse of innovative therapeutic paths to fight malaria. Blocking biosynthesis of UDP-GlcNAc in the parasites is another promising option to reduce Plasmodium life cycle.
MeSH term(s)	Acetylglucosamine/chemistry ; Acetylglucosamine/metabolism ; Glycosylation ; Plasmodium falciparum/chemistry ; Plasmodium falciparum/genetics ; Plasmodium falciparum/metabolism ; Protein Processing, Post-Translational ; Proteome ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism
Chemical Substances	Proteome ; Protozoan Proteins ; poly-N-acetyl glucosamine ; Acetylglucosamine (V956696549)
Language	English
Publishing date	2017-11-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1475-2875
ISSN (online)	1475-2875
DOI	10.1186/s12936-017-2131-2
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Article ; Online: Phosphorylation of Marburg virus matrix protein VP40 triggers assembly of nucleocapsids with the viral envelope at the plasma membrane.

Kolesnikova, Larissa / Mittler, Eva / Schudt, Gordian / Shams-Eldin, Hosam / Becker, Stephan

Cellular microbiology

2012 Volume 14, Issue 2, Page(s) 182–197

Abstract: Marburg virus (MARV) matrix protein VP40 plays a key role in virus assembly, recruiting nucleocapsids and the surface protein GP to filopodia, the sites of viral budding. In addition, VP40 is the only MARV protein able to induce the release of ... ...

Abstract	Marburg virus (MARV) matrix protein VP40 plays a key role in virus assembly, recruiting nucleocapsids and the surface protein GP to filopodia, the sites of viral budding. In addition, VP40 is the only MARV protein able to induce the release of filamentous virus-like particles (VLPs) indicating its function in MARV budding. Here, we demonstrated that VP40 is phosphorylated and that tyrosine residues at positions 7, 10, 13 and 19 represent major phosphorylation acceptor sites. Mutagenesis of these tyrosine residues resulted in expression of a non-phosphorylatable form of VP40 (VP40(mut) ). VP40(mut) was able to bind to cellular membranes, produce filamentous VLPs, and inhibit interferon-induced gene expression similarly to wild-type VP40. However, VP40(mut) was specifically impaired in its ability to recruit nucleocapsid structures into filopodia, and released infectious VLPs (iVLPs) had low infectivity. These results indicated that tyrosine phosphorylation of VP40 is important for triggering the recruitment of nucleocapsids to the viral envelope.
MeSH term(s)	Amino Acid Substitution ; Cell Line ; Cell Membrane/virology ; Humans ; Marburgvirus/physiology ; Mutagenesis, Site-Directed ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Nucleocapsid/metabolism ; Phosphorylation ; Protein Multimerization ; Tyrosine/metabolism ; Viral Matrix Proteins/genetics ; Viral Matrix Proteins/metabolism ; Virus Assembly
Chemical Substances	Mutant Proteins ; VP40 protein, virus ; Viral Matrix Proteins ; Tyrosine (42HK56048U)
Language	English
Publishing date	2012-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1468320-9
ISSN	1462-5822 ; 1462-5814
ISSN (online)	1462-5822
ISSN	1462-5814
DOI	10.1111/j.1462-5822.2011.01709.x
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Article ; Online: Functional and phylogenetic evidence of a bacterial origin for the first enzyme in sphingolipid biosynthesis in a phylum of eukaryotic protozoan parasites.

Mina, John G / Thye, Julie K / Alqaisi, Amjed Q I / Bird, Louise E / Dods, Robert H / Grøftehauge, Morten K / Mosely, Jackie A / Pratt, Steven / Shams-Eldin, Hosam / Schwarz, Ralph T / Pohl, Ehmke / Denny, Paul W

The Journal of biological chemistry

2017 Volume 292, Issue 29, Page(s) 12208–12219

Abstract: Toxoplasma ... ...

Abstract	Toxoplasma gondii
MeSH term(s)	Amino Acid Sequence ; Catalytic Domain ; Computational Biology ; Conserved Sequence ; Dimerization ; Endoplasmic Reticulum/enzymology ; Gene Deletion ; Gene Duplication ; Gene Transfer, Horizontal ; Isoenzymes/chemistry ; Isoenzymes/genetics ; Isoenzymes/isolation & purification ; Isoenzymes/metabolism ; Models, Molecular ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Phylogeny ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Transport ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Protozoan Proteins/isolation & purification ; Protozoan Proteins/metabolism ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; Serine C-Palmitoyltransferase/chemistry ; Serine C-Palmitoyltransferase/genetics ; Serine C-Palmitoyltransferase/isolation & purification ; Serine C-Palmitoyltransferase/metabolism ; Structural Homology, Protein ; Toxoplasma/enzymology
Chemical Substances	Isoenzymes ; Peptide Fragments ; Protozoan Proteins ; Recombinant Fusion Proteins ; Serine C-Palmitoyltransferase (EC 2.3.1.50)
Language	English
Publishing date	2017-06-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M117.792374
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