Understanding the surfactant dysfunction by gram-negative bacteria pulmonary infection, the intracellular fate of Chlamydia pneumoniae (Cpn), its interaction with uptake, recycling and secretion of surfactant and with the cytoskeleton of type II pneumocytes was investigated. Bacteria co-localized with SP-A-mediated endocytosed lipid and early endosomes (EEA1- and Rab5-positive) after 3 and 6 hours of infection. No specific contact with late endosomes (Rab7- and M6PR-positive), lysosomal or lamellar body markers (CD63, 3C9) was found after 12 hours of infection. In Cpn infected cells SP-A-mediated lipid uptake was significantly increased. After SP-A-mediated lipid uptake followed by "re-secretion", 90% of the internalized lipid remained intracellularly. SP-A and lipid did strongly co-localize with early endosomes. Internalized SP-A can not be re-secreted rapidly to plasma membrane, lipid is not transported toward late endosomes (Rab7- and M6PR-positive) or lamellar bodies (CD63- and 3C9-positive). These results indicate that increased surfactant internalization is caused by an inhibition in intracellular surfactant transport. Accumulation of SP-A-mediated lipid was associated with changes in -tubulin. Increases in surfactant secretion were associated with changes in F-actin. We postulate that Cpn infection of type II cells causes changes of the cytoskeleton and this effects are associated with alterations in intracellular transport and secretion of surfactant.