Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 495948
Title VAMP721a and VAMP721d are important for pectin dynamics and release of bacteria in soybean nodules
Author(s) Gavrin, Aleksandr; Chiasson, David; Ovchinnikova, Evgenia; Kaiser, B.N.; Bisseling, Ton; Fedorova, E.E.
Source New Phytologist (2016). - ISSN 0028-646X - p. 1011 - 1021.
DOI http://dx.doi.org/10.1111/nph.13837
Department(s) Laboratory of Molecular Biology
EPS
Publication type Refereed Article in a scientific journal
Publication year 2016
Keyword(s) Endosymbiosis - Exocytosis - Intracellular infection - Legume-rhizobia symbiosis - Plant cell wall - Soybean
Abstract

In root nodules rhizobia enter host cells via infection threads. The release of bacteria to a host cell is possible from cell wall-free regions of the infection thread. We hypothesized that the VAMP721d and VAMP721e exocytotic pathway, identified before in Medicago truncatula, has a role in the local modification of cell wall during the release of rhizobia. To clarify the role of VAMP721d and VAMP721e we used Glycine max, a plant with a determinate type of nodule. The localization of the main polysaccharide compounds of primary cell walls was analysed in control vs nodules with partially silenced GmVAMP721d. The silencing of GmVAMP721d blocked the release of rhizobia. Instead of rhizobia-containing membrane compartments - symbiosomes - the infected cells contained big clusters of bacteria embedded in a matrix of methyl-esterified and de-methyl-esterified pectin. These clusters were surrounded by a membrane. We found that GmVAMP721d-positive vesicles were not transporting methyl-esterified pectin. We hypothesized that they may deliver the enzymes involved in pectin turnover. Subsequently, we found that GmVAMP721d is partly co-localized with pectate lyase. Therefore, the biological role of VAMP721d may be explained by its action in delivering pectin-modifying enzymes to the site of release.

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