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van Antwerpen, P.

Publications and source records attributed to van Antwerpen, P..

2 recordsLinked to original sources

Phosphate Limitation Modulates Vibrio cholerae Outer Membrane Vesicle Formation, Composition and Toxicity

Vibrio cholerae inhabits phosphorus-poor aquatic environments and host intestine, where it expresses genes regulated by the PhoB/PhoR two-component system in response to inorganic phosphate (Pi) limitation. Like other Gram-negative bacteria, V. cholerae releases outer membrane vesicles (OMVs), which carry proteins, lipids, and nucleic acids that contribute to adaptation, survival, and pathogenesis. Here, we investigated how Pi availability affects OMV production, composition, and toxicity in the pandemic strain N16961 and its {Delta}phoB mutant. Using transmission electron microscopy, atomic force microscopy, and nanoparticle tracking analysis, we show that OMV size remains constant ([~]140 nm) across conditions, but production is significantly increased under Pi limitation in a PhoB-dependent manner. Proteomic and lipidomic analyses revealed selective packaging of PhoB-regulated proteins involved in phosphate metabolism, stress response, carbon metabolism, and toxicity, as well as enrichment in phosphorus-free ornithine lipids under low Pi. Functional assays in Galleria mellonella demonstrated that OMVs from N16961 under Pi limitation are highly toxic, whereas OMVs from high-Pi or {Delta}phoB cultures exhibit minimal lethality. Our findings indicate that phosphate limitation acts as an environmental cue that shapes OMV composition, enhancing both bacterial survival and pathogenic potential. This study highlights OMVs as dynamic vehicles integrating adaptation to low Pi concentration, stress adaptation, and toxicity in V. cholerae.

microbiology↗

Opposing roles for lipocalins and a CD36 family scavenger receptor in apical extracellular matrix-dependent protection of narrow tube integrity

All exposed epithelial surfaces, including the walls of internal tubes, are lined by a lipid and glycoprotein-rich apical extracellular matrix (aECM) that helps shape and protect the apical domain. Secreted lipocalins are lipid transporters frequently found within apical compartments. We show that loss of the C. elegans lipocalin LPR-1 disrupts the assembly of another lipocalin, LPR-3, within the pre-cuticle aECM that protects and shapes the narrow excretory duct and pore tubes. LPR-1 is apically secreted and colocalizes with LPR-3 in intracellular vesicles and lysosomes, but unlike LPR-3 it does not detectably incorporate into the aECM. Forward genetic screens for lpr-1 suppressors identified mutations in scav-2, which encodes a transmembrane protein of the CD36 scavenger receptor B family. Loss of scav-2 restored LPR-3 matrix localization and suppressed the lpr-1 tube shaping defect, as well as the tube-shaping defects of a subset of pre-cuticle mutants, but not lpr-3 mutants. A SCAV-2 fusion accumulated at apical surfaces of interfacial epithelial tubes, including the excretory duct and pore, and both tissue-specific suppression of lpr-1 matrix defects and tissue-specific rescue experiments support a local role for SCAV-2 within these tubes. These data demonstrate that LPR-1 and SCAV-2 have opposing effects on narrow tube integrity by altering the content and organization of that tubes luminal aECM, possibly by acting as transporters of an LPR-3 cofactor. These results have broadly relevant implications regarding the importance of lipocalins and scavenger receptors for aECM organization and integrity of the narrowest tubes in the body.

cell biology↗