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Open Access Research article

Absence of long-range diffusion of OmpA in E. coli is not caused by its peptidoglycan binding domain

Gertjan S Verhoeven12, Marileen Dogterom2 and Tanneke den Blaauwen13*

Author affiliations

1 Molecular Cytology, Swammerdam Institute for Life Sciences, University of Amsterdam, Science Park 904, Amsterdam, 1098 XH, The Netherlands

2 FOM Institute AMOLF, Science Park 104, Amsterdam, 1098 XG, The Netherlands

3 Bacterial Cell Biology, Swammerdam Institute for Life Sciences, University of Amsterdam, Sciencepark 904, Amsterdam, 1098 XH, The Netherlands

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Citation and License

BMC Microbiology 2013, 13:66  doi:10.1186/1471-2180-13-66

Published: 23 March 2013



It is widely believed that integral outer membrane (OM) proteins in bacteria are able to diffuse laterally in the OM. However, stable, immobile proteins have been identified in the OM of Escherichia coli. In explaining the observations, a hypothesized interaction of the immobilized OM proteins with the underlying peptidoglycan (PG) cell wall played a prominent role.


OmpA is an abundant outer membrane protein in E. coli containing a PG-binding domain. We use FRAP to investigate whether OmpA is able to diffuse laterally over long-range (> ~100 nm) distances in the OM. First, we show that OmpA, containing a PG binding domain, does not exhibit long-range lateral diffusion in the OM. Then, to test whether PG interaction was required for this immobilization, we genetically removed the PG binding domain and repeated the FRAP experiment. To our surprise, this did not increase the mobility of the protein in the OM.


OmpA exhibits an absence of long-range (> ~100 nm) diffusion in the OM that is not caused by its PG binding domain. Therefore, other mechanisms are needed to explain this observation, such as the presence of physical barriers in the OM, or strong interactions with other elements in the cell envelope.

Bacterial cell wall; Peptidoglycan; Outer membrane; Diffusion; FRAP; Cell membrane; OmpA