title: Chemosensory control of surface antigen switching in the nematode Caenorhabditis elegans.
abstract: Nematodes change their surface compositions in response to environmental signals, which may allow them to survive attacks from microbial pathogens or host immune systems. In the free-living species Caenorhabditis elegans, wild-type worms are induced to display an L1 (first larval stage) surface epitope at later larval stages when grown on an extract of spent culture medium (Inducible Larval Display or ILD). Before this study, it was not known whether ILD was regulated by the well-characterized, neurologically based chemical senses of C. elegans, which mediate other behavioural and developmental responses to environmental signals such as chemotaxis and formation of the facultatively arrested dauer larva stage. We show here that ILD requires the activities of three genes that are essential for the function of the C. elegans chemosensory neurons. ILD was abolished in chemotaxis-defective che-3, osm-3 and tax-4 mutants. In contrast, chemotaxis-defective mutants altered in a different gene, srf-6, show constitutive display of the L1 epitope on all four larval stages. The ILD-defective che-3, osm-3 and tax-4 mutations blocked the constitutive larval display of an srf-6 mutant. Combining srf-6 and certain dauer-constitutive mutations in double mutants enhanced constitutive dauer formation, consistent with the idea that srf-6 acts in parallel with specific components of the dauer formation pathway. These results taken together are consistent with the hypothesis that ILD is triggered by environmental signals detected by the nematode's chemosensory neurons.
authors.affiliation: Department of Biology and Biotechnology, Worcester Polytechnic Institute, Worcester, MA 01609, USA.
authors.forename: D P
authors.initials: DP
authors.lastname: Olsen
authors.forename: D
authors.initials: D
authors.lastname: Phu
authors.forename: L J M
authors.initials: LJ
authors.lastname: Libby
authors.forename: J A
authors.initials: JA
authors.lastname: Cormier
authors.forename: K M
authors.initials: KM
authors.lastname: Montez
authors.forename: E F
authors.initials: EF
authors.lastname: Ryder
authors.forename: S M
authors.initials: SM
authors.lastname: Politz
mesh_terms: D000818:Animals; D000954:Antigens, Surface / Q000235:genetics / Q000378:metabolism; D017173:Caenorhabditis elegans / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D029742:Caenorhabditis elegans Proteins / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D002628:Chemoreceptor Cells / Q000502:physiology*; D002630:Chemotactic Factors / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D002633:Chemotaxis / Q000502:physiology; D004398:Dyneins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D000939:Epitopes / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D018507:Gene Expression Regulation, Developmental / Q000276:immunology / Q000502:physiology*; D007473:Ion Channels / Q000235:genetics / Q000378:metabolism; D016547:Kinesins / Q000235:genetics / Q000378:metabolism; D007814:Larva / Q000254:growth & development / Q000276:immunology / Q000378:metabolism; D050505:Mutant Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D012867:Skin / Q000276:immunology / Q000378:metabolism; D012903:Smell / Q000502:physiology*
chemical_list: D000954:Antigens, Surface; D029742:Caenorhabditis elegans Proteins; D002630:Chemotactic Factors; D000939:Epitopes; D007473:Ion Channels; D050505:Mutant Proteins; C093002:OSM-3 protein, C elegans; C102184:tax-4 protein, C elegans; C522228:Che-3 protein, C elegans; D004398:Dyneins; D016547:Kinesins