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Meloidogyne javanica surface proteins: characterization and lability

Published online by Cambridge University Press:  01 November 1997

Y. SPIEGEL
Affiliation:
Department of Nematology, Agricultural Research Organization, The Volcani Center, Bet Dagan 50–250, Israel
I. KAHANE
Affiliation:
Department of Membrane and Ultrastructure Research, The Hebrew University, ‘Hadassah’ Medical School, Jerusalem, Israel
L. COHEN
Affiliation:
Department of Nematology, Agricultural Research Organization, The Volcani Center, Bet Dagan 50–250, Israel
E. SHARON
Affiliation:
Department of Nematology, Agricultural Research Organization, The Volcani Center, Bet Dagan 50–250, Israel

Abstract

Characterization of surface coat (SC) proteins including carbohydrate-binding proteins and glycoproteins of the plant-parasitic nematode Meloidogyne javanica 2nd-stage juvenile (J2) is reported. Extraction of surface proteins with sodiumdodecyl sulfate (SDS) and separation by denaturing polyacrylamide gel electrophoresis (SDS–PAGE) results with bandsat 6, 9, 14, 22, 26, 31, 46, 49, 58, 66, 80, 205 and 250 kDa. On Western blots, the neoglycoprotein, fucosylated-,mannosylated- and glucosylated-bovine serum albumin, reacted with the 14, 22, 26, 58 and 66 kDa bands. The lectins,Concanavalin A and wheat-germ agglutinin (WGA) labelled surface protein bands of 6, 9, 14, 31, 58 and 66 kDa; WGAalso labelled the 22 and 26 kDa bands. Biotin reagents were used to specifically trace surface proteins on live J2.SDS–PAGE of biotinylated J2 extracts revealed only 2 specific biotin-protein bands at 46 and 49 kDa. The labile andtransitory nature of Meloidogyne javanica SC was demonstrated by the dynamics of human red blood cells (HRBC)adherence to J2 of different ages. HRBC adherence was also used to demonstrate the SC recovery of detergent-treatedJ2, which was further exhibited in the SDS–PAGE profiles.

Type
Research Article
Copyright
1997 Cambridge University Press

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