J Appl Microbiol 2012, 113:560–568.PubMedCrossRef 44. Maloy SR, Stewart VJ, Tayler RK: Genetic analysis of pathogenic bacteria. New York: Cold Spring Harbor Press; 1996. 45. Watson PR, Paulin SM, Bland AP, Jones PW, Wallis TS: Characterization of intestinal invasion by Salmonella Typhimurium and Salmonella Dublin and the effect of a mutation in the invH gene. Infect Immun 1995, 63:2743–2754.PubMed 46. Chadfield MS, Brown DJ, Aabo S, Christensen JP, Olsen JE: Comparison of intestinal invasion and macrophage response of Salmonella Gallinarum and other host adapted Salmonella enterica serovars in the avian host. Vet Microbiol 2003, 92:49–64.PubMedCrossRef 47. Chadfield MS, Olsen JE: Determination of the oxidative burst

chemiluminescent response of avian and murine-derived macrophages versus corresponding cell-lines in relation to stimulation with Salmonella serovars. Vet Immunol Immunopathol selleck screening library 2001, 80:289–308.PubMedCrossRef 48. Jelsbak L, Thomsen LE, Wallrodt I, Jensen PR, Olsen JE: Polyamines are required for virulence in Salmonella enterica serovar Typhimurium. PLoS One 2012, 7:e36149.PubMedCrossRef Competing interests Selleck CRT0066101 The selleck chemicals authors declare that they have no competing interests. Authors’ contributions KH-H-A and JC constructed the strains, KH-HA, MSC and JEO conducted cell culture adhesion and invasion experiments,

MSC measured the oxidative response in macrophages, JEO measured cytokine responses, KH-HA, JEO and JR conducted mice challenge experiments, JEO drafted

the manuscript and all authors read and commented on this. All authors approved the final manuscript.”
“Background Little information exists on the mobility of (integral) outer membrane proteins (OMPs) in the bacterial OM. Traditionally, the bacterial outer membrane is presented as a tight, gel-like barrier, with LPS packed together with cations in a crystalline matrix [1, 2]. At the same time, experimental evidence suggests that integral outer membrane protein IcsA is able to diffuse laterally over micron-ranges in the OM [3]. Recent developments in live-cell protein labeling and (fluorescent) imaging technology are starting to elucidate the nature of protein dynamics in the bacterial OM. For example, recent work on the mobility of integral OMP LamB suggests that it is confined to a region of Amylase size ~50 nm [4, 5]. This was based on the motion of a marker bead or quantum dot attached to a surface-exposed biotinylated loop of LamB. The authors propose that the confinement is caused by LamB’s attachment to the peptidoglycan layer (PG) layer [6]. Furthermore, in pioneering experiments, proteins in the cell envelope of E. coli have been labeled using a reactive fluorescent dye [7, 8]. It was found that the mobility of (at least some) cell envelope proteins was restrained at the cellular poles [7]. Also, it was found that the cell envelope contained both mobile and immobile proteins [7, 8].