Jan Strauss

Dr. Jan Strauss

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Research Focus & Metrics

Academic Career Length

14Years (2013-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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8 September 2013 in Nature Climate Change
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ATA. Toseland
A. Toseland
SDS. J. Daines
S. J. Daines
JCJ. R. Clark
J. R. Clark
AKA. Kirkham
A. Kirkham
JSJan Strauss
Jan Strauss
Thomas UEAThomas UEA
Thomas UEA

16 January 2017 in Nature
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Journal Article
Open access
TMThomas Mock
Thomas Mock
RORobert P. Otillar
Robert P. Otillar
JSJan Strauss
Jan Strauss
MMMark McMullan
Mark McMullan
PPPirita Paajanen
Pirita Paajanen
Igor GrigorievIgor Grigoriev
Igor Grigoriev
The Southern Ocean houses a diverse and productive community of organisms. Unicellular eukaryotic diatoms are the main primary producers in this environment, where photosynthesis is limited by low concentrations of dissolved iron and large seasonal fluctuations in light, temperature and the extent of sea ice. How diatoms have adapted to this extreme environment is largely unknown. Here we present insights into the genome evolution of a cold-adapted diatom from the Southern Ocean, Fragilariopsis cylindrus, based on a comparison with temperate diatoms. We find that approximately 24.7 per cent of the diploid F. cylindrus genome consists of genetic loci with alleles that are highly divergent (15.1 megabases of the total genome size of 61.1 megabases). These divergent alleles were differentially expressed across environmental conditions, including darkness, low iron, freezing, elevated temperature and increased CO2. Alleles with the largest ratio of non-synonymous to synonymous nucleotide substitutions also show the most pronounced condition-dependent expression, suggesting a correlation between diversifying selection and allelic differentiation. Divergent alleles may be involved in adaptation to environmental fluctuations in the Southern Ocean.

27 August 2019 in mBio
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Journal Article
Open access
JWJ. Stephan Wichers
J. Stephan Wichers
JSJudith A. M. Scholz
Judith A. M. Scholz
JSJan Strauss
Jan Strauss
SWSusanne Witt
Susanne Witt
ALAndrés Lill
Andrés Lill
ABAnna Bachmann
Anna Bachmann
Malaria claims about half a million lives each year. Plasmodium falciparum , the causative agent of the most severe form of the disease, uses proteins that are translocated to the surface of infected erythrocytes for immune evasion. To circumvent the detection of these gene products by the immune system, the parasite evolved a complex strategy that includes gene duplications and elaborate sequence polymorphism. STEVORs are one family of these variant surface antigens and are encoded by about 40 genes. Using deep RNA sequencing of blood-stage parasites, including free merozoites, we first established stevor expression of the cultured isolate and compared it with published transcriptomes. We reveal a biphasic expression of most stevor genes and confirm this for individual STEVORs at the protein level. The membrane topology of a rhoptry-associated variant was experimentally elucidated and linked to host cell invasion, underlining the importance of this multifunctional protein family for parasite proliferation.

15 January 2019 in Journal of the American Chemical Society
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YUYonca Ural-Blimke
Yonca Ural-Blimke
AFAli Flayhan
Ali Flayhan
JSJan Strauss
Jan Strauss
VRVasileios Rantos
Vasileios Rantos
KBKim Bartels
Kim Bartels
CLChristian Löw
Christian Löw
Members of the solute carrier 15 family (SLC15) transport di- and tripeptides as well as peptidomimetic drugs across the cell membrane. Structures of bacterial homologues have provided valuable information on the binding and transport of their natural substrates, but many do not transport medically relevant drugs. In contrast, a homologue from Escherichia coli, DtpA, shows a high similarity to human PepT1 (SLC15A1) in terms of ligand selectivity and transports a similar set of drugs. Here, we present the crystal structure of DtpA in ligand-free form (at 3.30 Å resolution) and in complex with the antiviral prodrug valganciclovir (at 2.65 Å resolution) supported by biochemical data. We show that valganciclovir unexpectedly binds with the ganciclovir moiety mimicking the N-terminal residue of a canonical peptide substrate. Based on a homology model we argue that this binding mode also applies to the human PepT1 transporter. Our results provide new insights into the binding mode of prodrugs and will assist the rational design of drugs with improved absorption rates.

18 January 2018 in The ISME Journal
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SAShazia N. Aslam
Shazia N. Aslam
JSJan Strauss
Jan Strauss
DTDavid Thomas
David Thomas
Thomas UEAThomas UEA
Thomas UEA
GUGraham J. C. Underwood
Graham J. C. Underwood
Diatoms are significant primary producers in sea ice, an ephemeral habitat with steep vertical gradients of temperature and salinity characterizing the ice matrix environment. To cope with the variable and challenging conditions, sea ice diatoms produce polysaccharide-rich extracellular polymeric substances (EPS) that play important roles in adhesion, cell protection, ligand binding and as organic carbon sources. Significant differences in EPS concentrations and chemical composition corresponding to temperature and salinity gradients were present in sea ice from the Weddell Sea and Eastern Antarctic regions of the Southern Ocean. To reconstruct the first metabolic pathway for EPS production in diatoms, we exposed Fragilariopsis cylindrus, a key bi-polar diatom species, to simulated sea ice formation. Transcriptome profiling under varying conditions of EPS production identified a significant number of genes and divergent alleles. Their complex differential expression patterns under simulated sea ice formation was aligned with physiological and biochemical properties of the cells, and with field measurements of sea ice EPS characteristics. Thus, the molecular complexity of the EPS pathway suggests metabolic plasticity in F. cylindrus is required to cope with the challenging conditions of the highly variable and extreme sea ice habitat.

8 April 2021 in Cellular Microbiology
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Journal Article
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JWJan Stephan Wichers
Jan Stephan Wichers
JWJuliane Wunderlich
Juliane Wunderlich
DHDorothee Heincke
Dorothee Heincke
SPSamuel Pazicky
Samuel Pazicky
JSJan Strauss
Jan Strauss
TGTim W. Gilberger
Tim W. Gilberger
The inner membrane complex (IMC) is a defining feature of apicomplexan parasites, which confers stability and shape to the cell, functions as a scaffolding compartment during the formation of daughter cells and plays an important role in motility and invasion during different life cycle stages of these single celled organisms. To explore the IMC proteome of the malaria parasite Plasmodium falciparum we applied a proximity‐dependent biotin identification (BioID)‐based proteomics approach, using the established IMC marker protein Photosensitized INA‐Labelled protein 1 (PhIL1) as bait in asexual blood‐stage parasites. Subsequent mass spectrometry‐based peptide identification revealed enrichment of twelve known IMC proteins and several uncharacterized candidate proteins. We validated nine of these previously uncharacterized proteins by endogenous GFP‐tagging. Six of these represent new IMC proteins, while three proteins have a distinct apical localization that most likely represent structures described as apical annuli in Toxoplasma gondii. Additionally, various Kelch13 interacting candidates were identified, suggesting an association of the Kelch13 compartment and the IMC in schizont and merozoite stages. This work extends the number of validated IMC proteins in the malaria parasite and reveals for the first time the existence of apical annuli proteins in P. falciparum. Additionally, it provides evidence for a spatial association between the Kelch13 compartment and the IMC in late blood‐stage parasites.