Stepwise folding of an autotransporter passenger domain is not essential for its secretion.

Autotransporters are a superfamily of virulence proteins produced by Gram-negative bacteria. They consist of an N-terminal β-helical domain ("passenger domain") that is secreted into the extracellular space and a C-terminal β-barrel domain ("β-domain") that anchors the protein to the outer membrane. Because the periplasm lacks ATP, vectorial folding of the passenger domain in a C-to-N-terminal direction has been proposed to drive the secretion reaction.

Charge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.

Autotransporters are a large class of virulence proteins produced by Gram-negative bacteria. They contain an N-terminal extracellular ("passenger") domain that folds into a β-helical structure and a C-terminal β-barrel ("β") domain that anchors the protein to the outer membrane. Because the periplasm lacks ATP, the source of energy that drives passenger domain secretion is unknown.

NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes.

Following a blood meal, the mosquito Aedes aegypti will have acquired an enormous sodium load that must be rapidly excreted to restore ion homeostasis. It is a process that demands robust sodium and fluid transport capabilities. Even though the identities of the components involved in this ion transport across the mosquito Malpighian tubule epithelia have not been completely determined, electrophysiological studies suggest the contribution of a Na(+)/H(+) exchanger extruding cations into the lumen driven secondarily by the proton gradient created by the V-type H(+)-ATPase in the tubules' apical membrane.

Molecular characterization of sodium/proton exchanger 3 (NHE3) from the yellow fever vector, Aedes aegypti.

Transport across insect epithelia is thought to depend on the activity of a vacuolar-type proton ATPase (V-ATPase) that energizes ion transport through a secondary proton/cation exchanger. Although several of the subunits of the V-ATPase have been cloned, the molecular identity of the exchanger has not been elucidated. Here, we present the identification of sodium/proton exchanger isoform 3 (NHE3) from yellow fever mosquito, Aedes aegypti (AeNHE3).