Rhizobium Leguminosarum Biovars Secrete Several Homologous Epsbinding Proteins Into The Environment

N. Ausmees, M. Lindberg

Dept of Microbiology, Swedish University of Agricultural Sciences, SLU, Uppsala, Sweden 1. Introduction

Using phage display technique we identified a family of secreted proteins in R. leguminosarum, which interact with the bacterial cell surface (Ausmees et al. 2001). These proteins (RapAl, -A2, -A3, RapB and RapC) and some others (PlyA and PlyB, Finnie et al. 1998) contain one or several so-called Ra-domains, which are responsible for this binding (Figure 1). Here we show that the Ra-domain specifically recognizes a carbohydrate epitope of EPS and CPS of i?, leguminosarum.

PlyA PlyB Endoglucanase activity, heptapeptide repeats RapAl, -A2, -A3 At least three alleles in the genome

RapB _Similarity to an endoglucanase

'WTH'* sequence not available, size -60 kDa

Figure 1. Domain architecture of proteins containing Ra-domains (boxes).

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