Lectin-like glycoprotein PsNLEC-1 is not correctly glycosylated and targeted in boron-deficient pea nodules

Molecular Plant-microbe Interactions : MPMI
Luis BolañosI Bonilla

Abstract

Symbiosome development was studied in pea root nodules from plants growing in the absence of boron (B). Rhizobia released into the host cells of nodules from B-deficient plants developed to abnormal endophytic forms with an altered electrophoretic lipopolysaccharide pattern. Immunostaining after sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electroblotting of nodule homogenates with antibodies that recognize glycoprotein components showed that two previously described lectin-like glycoproteins (PsNLEC-1A and PsNLEC-1B) did not harbor the carbohydrate epitope normally recognized by specific monoclonal antibodies. Material derived from B-deficient nodules, however, still contained three antigenic isoforms with similar electrophoretic mobilities to PsNLEC-1 isoforms A, B, and C. These could be detected following immunoblotting and immunostaining with a specific antiserum originating from the purified PsNLEC protein that had been heterologously expressed in Escherichia coli. Immunogold localization of PsNLEC-1 sugar epitopes in B-deficient nodules showed that they were associated mostly with cytoplasmic vesicles rather than normal localization in the symbiosome compartment of mature infected cells. These results sug...Continue Reading

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Citations

May 30, 2009·Plant & Cell Physiology·Monika A WimmerHeiner E Goldbach
Sep 4, 2012·Plant & Cell Physiology·Jesús MontielCarmen Quinto
Oct 15, 2011·Molecular Plant-microbe Interactions : MPMI·Attila KeresztEva Kondorosi
Aug 20, 2015·International Journal of Molecular Sciences·Bargaz AdnaneCarlsson Georg
Nov 20, 2008·Journal of Integrative Plant Biology·Juan J Camacho-CristóbalAgustín González-Fontes
Feb 8, 2005·Plant Physiology and Biochemistry : PPB·Luis BolañosDale Blevins

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