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ProteomicsQuantitative analysis of proteomic changes induced by potential quorum sensing in Haloferax volcanii
Quorum sensing (QS) is a mechanism of intercellular communication that enables microbes to alter gene expression and adapt to the environment. While QS has been extensively studied in bacteria, little is known about cell-cell communication in archaea. We could show that for Haloferax volcanii, the t...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) Archaea 
2025-06-17 | PXD059278 | Pride
Archaeal proteome project Ursgal Archaea Haloferax volcanii Label-free quantification Quorum sensing Cell shape 
ProteomicsComparative, quantitative proteomic analysis of cell shape transitions in Haloferax volcanii
Cell shape plays a crucial role in microbial survival. While Haloferax volcanii, a model haloarchaeon, forms rods and disks, depending on environmental conditions, little is known about mechanisms underpinning archaeal cell-shape determination. We identified mutants that exclusively form rods and ca...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) Archaea 
2024-02-17 | PXD040781 | Pride
Archaeal proteome project Ursgal Archaea Haloferax volcanii Label-free quantification Cell shape 
ProteomicsGlycoproteomic analysis of Haloferax volcanii strains H53, DaglB, and Dagl15
An in-depth glycoproteomic analysis of Haloferax volcanii has been performed, comparing the wildtype H53 with knockout mutants of aglB and agl15. While AglB-dependent glycosylation has been described to occur under standard culture conditions, the Agl15-dependent glycosylation pathway has previously...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) 
2021-06-20 | PXD021874 | Pride
Glycoproteomics Glycosylation Archaea Haloferax volcanii 
ProteomicsCharacterizing of Haloferax volcanii Hvo_0405 as a Tat substrate
In order to test the hypothesis that Hvo_0405 is a Tat substrate, samples from the membrane and cytoplasm of strains expressing Hvo_0405RR or the mutated Hvo_0405KK were analyzed by mass spectrometry. A semi-enzymatic peptid corresponding to the cleavage of the signal peptide could only be identifie...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) 
2020-05-11 | PXD010824 | Pride
Archaea Twin-arginine translocation Haloferax volcanii Archaeosortase 
ProteomicsCharacterizing N-Glycosylation of Pilins and Flagellins from Haloferax volcanii
Mass spectrometric analysis of cesium chloride purified flagellins and pilins confirmed previously identified N-glycopeptides for FlgA1, revealed additional N-glycopeptides for FlgA1 and FlgA2 and characterized N-glycosylation of PilA1 and PilA2. Analyses were performed using different MS methods (w...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) 
2020-05-11 | PXD011015 | Pride
Archaea Haloferax volcanii N-glycosylation Type iv pili Flagella 
ProteomicsQuantitative (Glyco-)Proteomics of Haloferax volcanii Biofilm Formation
A quantitative proteomics analysis comparing planktonic and sessile cells at different stages of biofilm development, using iTRAQ labeling, has been performed for Haloferax volcanii. Samples were taken from liquid, shaking cultures were compared to samples from static cultures, separated into sessil...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) 
2020-05-11 | PXD011012 | Pride
Glycosylation Haloferax volcanii Biofilm Itraq 
ProteomicsMass spectrometric analysis of proteolytic cleavage related to ArtA and PssA from Haloferax volcanii
The S-layer glycoprotein (SLG) of Haloferax volcanii has been shown to be processed and C-terminally linked to a lipid in an archaeosortase A (ArtA)-dependent manner. A C-terminal tripartite structure including a PGF motif is required for the processing of SLG as well as other substrates (Abdul Hali...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) 
2020-05-11 | PXD011050 | Pride
Haloferax volcanii Lipid anchoring Archaeosortase S-layer glycoprotein 
ProteomicsQuantitative analysis of lipoproteins from Haloferax volcanii using aliA and aliB deletion mutants
This project aimed to analyze protein lipidation, a widespread strategy for anchoring proteins to cellular membranes across all domains of life, in the model archaeon Haloferax volcanii. Using deletion mutants of aliA and aliB, the first archaeal enzymes shown to be involved in lipobox-containing pr...
ORGANISM(S): Haloferax volcanii (Halobacterium volcanii) 
2026-08-18 | PXD074718 | Pride
Haloferax volcanii Archaea Triton x-114 Lipoproteins 
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