A gene family of cathepsin L-like proteases of filarial nematodes are associated with larval molting and cuticle and eggshell remodeling

David B. Guiliano, Xiqiang Hong, James H. McKerrow, Mark L. Blaxter, Yelena Oksov, Jing Liu, Elodie Ghedin, Sara Lustigman

Research output: Contribution to journalArticle

Abstract

Cysteine proteinases are involved in a variety of important biological processes and have been implicated in molting and tissue remodeling in free living and parasitic nematodes. We show that in the lymphatic filarial nematode Brugia pahangi molting of third-stage larvae (L3) to fourth-stage larvae is dependent on the activity of a cathepsin L-like cysteine protease (CPL), which can be detected in the excretory/secretory (ES) products of molting L3. Directed cloning of a cysteine protease gene in B. pahangi and analysis of the expressed sequence tag (EST) and genomic sequences of the closely related human lymphatic filarial nematode Brugia malayi have identified a family of CPLs. One group of these enzymes, Bm-cpl-1, -4, -5 and Bp-cpl-4, is highly expressed in the B. malayi and B. pahangi infective L3 larvae. Immunolocalization indicates that the corresponding enzymes are synthesized and stored in granules of the glandular esophagus of L3 and released during the molting process. Functional analysis of these genes in Brugia and closely related CPL genes identified in the filarial nematode Onchocerca volvulus and the free living model nematode Caenorhabditis elegans indicate that these genes are also involved in cuticle and eggshell remodeling.

Original languageEnglish (US)
Pages (from-to)227-242
Number of pages16
JournalMolecular and Biochemical Parasitology
Volume136
Issue number2
DOIs
StatePublished - Aug 2004

Fingerprint

Egg Shell
Cathepsin L
Molting
Brugia pahangi
Cysteine Proteases
Peptide Hydrolases
Brugia malayi
Larva
Genes
Brugia
Onchocerca volvulus
Biological Phenomena
Expressed Sequence Tags
Caenorhabditis elegans
Enzymes
Esophagus
Organism Cloning

Keywords

  • 7-amino-4-methylcoumarin
  • AMC
  • benzyloxycarbonyl
  • cathepsin L-like cysteine protease
  • cathepsin Z-like cysteine protease
  • CPF
  • CPL
  • CPZ
  • ES
  • EST
  • excretory/secretory
  • expressed sequence tag
  • fluoromethyl ketone
  • FMK
  • fourth-stage larvae
  • L3
  • L4
  • third-stage larvae
  • Z

ASJC Scopus subject areas

  • Molecular Biology
  • Parasitology

Cite this

A gene family of cathepsin L-like proteases of filarial nematodes are associated with larval molting and cuticle and eggshell remodeling. / Guiliano, David B.; Hong, Xiqiang; McKerrow, James H.; Blaxter, Mark L.; Oksov, Yelena; Liu, Jing; Ghedin, Elodie; Lustigman, Sara.

In: Molecular and Biochemical Parasitology, Vol. 136, No. 2, 08.2004, p. 227-242.

Research output: Contribution to journalArticle

Guiliano, David B. ; Hong, Xiqiang ; McKerrow, James H. ; Blaxter, Mark L. ; Oksov, Yelena ; Liu, Jing ; Ghedin, Elodie ; Lustigman, Sara. / A gene family of cathepsin L-like proteases of filarial nematodes are associated with larval molting and cuticle and eggshell remodeling. In: Molecular and Biochemical Parasitology. 2004 ; Vol. 136, No. 2. pp. 227-242.
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AB - Cysteine proteinases are involved in a variety of important biological processes and have been implicated in molting and tissue remodeling in free living and parasitic nematodes. We show that in the lymphatic filarial nematode Brugia pahangi molting of third-stage larvae (L3) to fourth-stage larvae is dependent on the activity of a cathepsin L-like cysteine protease (CPL), which can be detected in the excretory/secretory (ES) products of molting L3. Directed cloning of a cysteine protease gene in B. pahangi and analysis of the expressed sequence tag (EST) and genomic sequences of the closely related human lymphatic filarial nematode Brugia malayi have identified a family of CPLs. One group of these enzymes, Bm-cpl-1, -4, -5 and Bp-cpl-4, is highly expressed in the B. malayi and B. pahangi infective L3 larvae. Immunolocalization indicates that the corresponding enzymes are synthesized and stored in granules of the glandular esophagus of L3 and released during the molting process. Functional analysis of these genes in Brugia and closely related CPL genes identified in the filarial nematode Onchocerca volvulus and the free living model nematode Caenorhabditis elegans indicate that these genes are also involved in cuticle and eggshell remodeling.

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