Identification and Characterization of the Most Abundant Cellulases in Stylet Secretions from Globodera rostochiensis (2023)

Rehman, S., Butterbach, P. B. E., Popeijus, H. E., Overmars, H. A., Davis, E. L., Jones, J. T., Goverse, A., Bakker, J. (2009). Identification and Characterization of the Most Abundant Cellulases in Stylet Secretions from Globodera rostochiensis. Phytopathology, 99(2), 194-202. https://doi.org/10.1094/PHYTO-99-2-0194

Rehman, S. ; Butterbach, P.B.E. ; Popeijus, H.E. et al. / Identification and Characterization of the Most Abundant Cellulases in Stylet Secretions from Globodera rostochiensis. In: Phytopathology. 2009 ; Vol. 99, No. 2. pp. 194-202.

@article{c92680b5e5424d488a24753e0e196f92,

title = "Identification and Characterization of the Most Abundant Cellulases in Stylet Secretions from Globodera rostochiensis",

abstract = "Plant-parasitic cyst nematodes secrete cell wall modifying proteins during their invasion of host plants. In this study, we used a monoclonal antibody to immunopurify and to sequence the N terminus of the most abundant cellulases in stylet secretions of preparasitic juveniles of Globodera rostochiensis. The N-terminal amino acid sequence perfectly matched the sequence of an expressed sequence tag of two nearly identical genes, named Gr-eng3 and Gr-eng4, which show relatively low similarity with the previously identified Gr-eng1 and Gr-eng2 (i.e., 62% similarity and 42% identity). The recombinantly produced proteins from Gr-eng3 and Gr-eng4 demonstrated specific activity on carboxymethylcellulose, indicating that these genes encode active cellulases. To date, the cellulases in cyst nematodes are comprised of three possible domain structure variants with different types of ancillary domains at the C terminus of the glycosyl hydrolase family 5 (GHF5) domain. We used Bayesian inference to show that the phylogeny of the GHF5 domain based on currently available data suggest that the extant nematode cellulases arose through reshuffling of the GHF5 domain with different types of ancillary domains as relatively independent units. Knocking-down Gr-eng3 and Gr-eng4 using RNA interference resulted in a reduction of nematode infectivity by 57%. Our observations show that the reduced infectivity of the nematodes can be attributed to poor penetration of the host's root system at the onset of parasitism",

keywords = "potato cyst-nematode, heterodera-glycines, meloidogyne-incognita, cell-walls, beta-1,4-endoglucanase genes, expression, degradation, proteins, origin, parasitism",

author = "S. Rehman and P.B.E. Butterbach and H.E. Popeijus and H.A. Overmars and E.L. Davis and J.T. Jones and A. Goverse and J. Bakker and G. Smant",

year = "2009",

doi = "10.1094/PHYTO-99-2-0194",

language = "English",

volume = "99",

pages = "194--202",

journal = "Phytopathology",

issn = "0031-949X",

publisher = "American Phytopathological Society",

number = "2",

}

Rehman, S, Butterbach, PBE, Popeijus, HE, Overmars, HA, Davis, EL, Jones, JT, Goverse, A, Bakker, J 2009, 'Identification and Characterization of the Most Abundant Cellulases in Stylet Secretions from Globodera rostochiensis', Phytopathology, vol. 99, no. 2, pp. 194-202. https://doi.org/10.1094/PHYTO-99-2-0194

Identification and Characterization of the Most Abundant Cellulases in Stylet Secretions from Globodera rostochiensis. / Rehman, S.; Butterbach, P.B.E.; Popeijus, H.E. et al.
In: Phytopathology, Vol. 99, No. 2, 2009, p. 194-202.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - Identification and Characterization of the Most Abundant Cellulases in Stylet Secretions from Globodera rostochiensis

AU - Rehman, S.

AU - Butterbach, P.B.E.

AU - Popeijus, H.E.

AU - Overmars, H.A.

AU - Davis, E.L.

AU - Jones, J.T.

AU - Goverse, A.

AU - Bakker, J.

AU - Smant, G.

PY - 2009

Y1 - 2009

N2 - Plant-parasitic cyst nematodes secrete cell wall modifying proteins during their invasion of host plants. In this study, we used a monoclonal antibody to immunopurify and to sequence the N terminus of the most abundant cellulases in stylet secretions of preparasitic juveniles of Globodera rostochiensis. The N-terminal amino acid sequence perfectly matched the sequence of an expressed sequence tag of two nearly identical genes, named Gr-eng3 and Gr-eng4, which show relatively low similarity with the previously identified Gr-eng1 and Gr-eng2 (i.e., 62% similarity and 42% identity). The recombinantly produced proteins from Gr-eng3 and Gr-eng4 demonstrated specific activity on carboxymethylcellulose, indicating that these genes encode active cellulases. To date, the cellulases in cyst nematodes are comprised of three possible domain structure variants with different types of ancillary domains at the C terminus of the glycosyl hydrolase family 5 (GHF5) domain. We used Bayesian inference to show that the phylogeny of the GHF5 domain based on currently available data suggest that the extant nematode cellulases arose through reshuffling of the GHF5 domain with different types of ancillary domains as relatively independent units. Knocking-down Gr-eng3 and Gr-eng4 using RNA interference resulted in a reduction of nematode infectivity by 57%. Our observations show that the reduced infectivity of the nematodes can be attributed to poor penetration of the host's root system at the onset of parasitism

AB - Plant-parasitic cyst nematodes secrete cell wall modifying proteins during their invasion of host plants. In this study, we used a monoclonal antibody to immunopurify and to sequence the N terminus of the most abundant cellulases in stylet secretions of preparasitic juveniles of Globodera rostochiensis. The N-terminal amino acid sequence perfectly matched the sequence of an expressed sequence tag of two nearly identical genes, named Gr-eng3 and Gr-eng4, which show relatively low similarity with the previously identified Gr-eng1 and Gr-eng2 (i.e., 62% similarity and 42% identity). The recombinantly produced proteins from Gr-eng3 and Gr-eng4 demonstrated specific activity on carboxymethylcellulose, indicating that these genes encode active cellulases. To date, the cellulases in cyst nematodes are comprised of three possible domain structure variants with different types of ancillary domains at the C terminus of the glycosyl hydrolase family 5 (GHF5) domain. We used Bayesian inference to show that the phylogeny of the GHF5 domain based on currently available data suggest that the extant nematode cellulases arose through reshuffling of the GHF5 domain with different types of ancillary domains as relatively independent units. Knocking-down Gr-eng3 and Gr-eng4 using RNA interference resulted in a reduction of nematode infectivity by 57%. Our observations show that the reduced infectivity of the nematodes can be attributed to poor penetration of the host's root system at the onset of parasitism

KW - potato cyst-nematode

KW - heterodera-glycines

KW - meloidogyne-incognita

KW - cell-walls

KW - beta-1,4-endoglucanase genes

KW - expression

KW - degradation

KW - proteins

KW - origin

KW - parasitism

U2 - 10.1094/PHYTO-99-2-0194

DO - 10.1094/PHYTO-99-2-0194

M3 - Article

SN - 0031-949X

VL - 99

SP - 194

EP - 202

JO - Phytopathology

JF - Phytopathology

IS - 2

ER -

Rehman S, Butterbach PBE, Popeijus HE, Overmars HA, Davis EL, Jones JT et al. Identification and Characterization of the Most Abundant Cellulases in Stylet Secretions from Globodera rostochiensis. Phytopathology. 2009;99(2):194-202. doi: 10.1094/PHYTO-99-2-0194