Caenorhabditis elegans as a model for parasitic nematodes: A focus on the cuticle

Politz, Samuel M.; Philipp, Mario T.

doi:10.1016/0169-4758(92)90302-i

Cited by 93 publications

(48 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The free-living nematode Caenorhabditis elegans has long been proposed as a genetic 269 and experimentally amenable model nematode system (Politz and Philipp, 1992 (Hawdon et al, 2003) and A. ceylanicum (Milstone et al, 2000). Indeed, the A. ceylanicum 293 inhibitor was also localized to the sub-cuticle of the adult stages (Chu et al, 2004).…”

Section: Discussion 267 268mentioning

confidence: 99%

Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: Identification and characterization of a novel serine protease inhibitor

Page

McCormack

Birnie

2006

International Journal for Parasitology

View full text Add to dashboard Cite

The nematode Caenorhabditis elegans represents an excellent model in which to examine nematode gene expression and function. A completed genome, straightforward transgenesis, available mutants and practical genome-wide RNAi approaches provide an invaluable toolkit in the characterization of nematode genes. We have performed a targeted RNAi screen in an attempt to identify components of the cuticle collagen biosynthetic pathway. Collagen biosynthesis and cuticle assembly are multi-step processes that involve numerous key enzymes involved in post-translational modification, trimer folding, procollagen processing and subsequent cross-linking stages. Many of these steps, the modifications and the enzymes are unique to nematodes and may represent attractive targets for the control of parasitic nematodes. A novel serine protease inhibitor was uncovered during our targeted screen, which is involved in collagen maturation, proper cuticle assembly and the moulting process. We have confirmed a link between this inhibitor and the

show abstract

Section: Discussion 267 268mentioning

confidence: 99%

Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: Identification and characterization of a novel serine protease inhibitor

Page

McCormack

Birnie

2006

International Journal for Parasitology

View full text Add to dashboard Cite

show abstract

“…Mutations in bah-1, bah-2, bah-3, bus-2, bus-4, bus-12, bus-17, srf-2, srf-3, and srf-5 each confer resistance to Yersinia biofilms (13), and C. elegans worms carrying these mutations are completely resistant to X. nematophila biofilms (Table 3). These mutations are known to alter the C. elegans surface (13,27,28,30,35,40,(48)(49)(50). Mutations in srf-4, srf-6, and srf-8 conferred partial resistance to biofilm accumulation (Table 3).…”

Section: Resultsmentioning

confidence: 99%

ThehmsHFRSOperon ofXenorhabdus nematophilaIs Required for Biofilm Attachment toCaenorhabditis elegans

Drace

Darby

2008

Appl Environ Microbiol

View full text Add to dashboard Cite

The bacterium Xenorhabdus nematophila is an insect pathogen and an obligate symbiont of the nematode Steinernema carpocapsae. X. nematophila makes a biofilm that adheres to the head of the model nematode Caenorhabditis elegans, a capability X. nematophila shares with the biofilms made by Yersinia pestis and Yersinia pseudotuberculosis. As in Yersinia spp., the X. nematophila biofilm requires a 4-gene operon, hmsHFRS. Also like its Yersinia counterparts, the X. nematophila biofilm is bound by the lectin wheat germ agglutinin, suggesting that ␤-linked N-acetyl-D-glucosamine or N-acetylneuraminic acid is a component of the extracellular matrix. C. elegans mutants with aberrant surfaces that do not permit Yersinia biofilm attachment also are resistant to X. nematophila biofilms. An X. nematophila hmsH mutant that failed to make biofilms on C. elegans had no detectable defect in symbiotic association with S. carpocapsae, nor was virulence reduced against the insect Manduca sexta.The gram-negative enterobacterium Xenorhabdus nematophila is an obligate symbiont of the entomopathogenic nematode Steinernema carpocapsae (24,25,33). The only free-living stage of the nematode, the infective juvenile (IJ) stage, carries a microcolony of X. nematophila cells in an intestinal compartment known as the bacterial receptacle (19,42,43,54). Once a suitable insect prey is found, S. carpocapsae invades the host and releases the bacteria. X. nematophila proliferates, suppresses insect immunity, and secretes insecticidal toxins that kill the host, while the nematode completes a few generations of reproduction utilizing the bacteria and host tissue for nutrients. When resources are depleted within the corpse, the nematodes reassociate with the bacteria, and a population of newly colonized IJs exits the host to begin the cycle again (16,21,38).The dual interactions with invertebrates-an intimate symbiosis and a potent pathogenicity-make X. nematophila an excellent model for investigating the mechanisms of mutualistic versus virulent associations (25,33,43). Several factors, including some involved in transcriptional regulation or nutrient acquisition, have been demonstrated to play roles in both symbiotic and pathogenic behaviors of X. nematophila and other bacterial species (8,12,26,31,32).Diverse bacteria contain homologous 4-gene operons involved in biofilm formation. The genes and their products were first characterized in Staphylococcus epidermidis, in which the icaADBC operon is required for biofilms that contain polysaccharide intercellular adhesin (PIA) (22,29,41). The major constituent of PIA is a ␤-1,6-linked homopolymer of N-acetyl-D-glucosamine (GlcNAc) synthesized by the glycosyltransferase IcaA (22). In Yersinia pestis, the hmsHFRS operon is necessary for biofilm-mediated colonization of fleas (37). Antibodies raised against S. epidermidis PIA react with Y. pestis exopolysaccharide (4), suggesting overlapping compositions. Similar operons are also found in Escherichia coli, Bordetella spp., Actinobacillus spp., Xanthomonas ...

show abstract

“…These proteins have been termed 'cuticlins' (Politz & Philipp, 1992), and are resistant to collagenase, which specifically cleaves the Gly-X bond within the (Gly-X-Y) n repetitive motif of collagens. Despite the fact that we used antisera raised against such epicuticular components to screen a cDNA library of adult B. pahangi, mainly collagens were identified by this approach.…”

Section: Discussionmentioning

confidence: 99%

Identification and sequence comparison of a cuticular collagen ofBrugia pahangi

Bisoffi

Betschart²

1996

Parasitology

View full text Add to dashboard Cite

SUMMARYThe cuticle of filarial nematodes is a specialized extracellular matrix that covers the parasite and protects it from adverse conditions of the environment. As a surface structure it is in direct contact with the host defence mechanisms and therefore plays an important role in the molecular host-parasite relationship. Using polyclonal antisera raised against the insoluble components of the cuticle of the adult filarial parasite Brugia pahangi, we have isolated cDNA clones encoding collagen molecules of the cuticle. The protein domain structure of cDNA clone Bpcol-1 was compared with the known structures of cuticular collagens of the nematodes Brugia malayi, Caenorhabditis elegans, Ascaris suum and Haemonchus contortus, confirming interspecies similarities. Using affinity-purified anti-Bpcol-1 antibodies we identified Bpcol-1 antigenic determinants in different nematode extracts, and determined the localization of such epitopes within the cuticle of B. pahangi.

show abstract

Caenorhabditis elegans as a model for parasitic nematodes: A focus on the cuticle

Cited by 93 publications

References 47 publications

Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: Identification and characterization of a novel serine protease inhibitor

Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: Identification and characterization of a novel serine protease inhibitor

ThehmsHFRSOperon ofXenorhabdus nematophilaIs Required for Biofilm Attachment toCaenorhabditis elegans

Identification and sequence comparison of a cuticular collagen ofBrugia pahangi

Contact Info

Product

Resources

About