Surfactant protein D (
SP-D) is a collagenous
calcium-dependent
lectin constitutively expressed by alveolar type II pneumocytes and non-ciliated bronchiolar epithelial (Clara) cells. It binds to surface
glycoconjugates expressed by a wide variety of microorganisms such as Gram-negative bacteria, influenza A virus, and various fungi, leading to pathogen inactivation or enhanced neutrophil and macrophage activity. Since a hallmark of
bronchopneumonia is the initiation of
inflammation in the bronchi and bronchoalveolar junction, we chose a classic ruminant model of
bronchopneumonia caused by Mannheimia haemolytica to study the expression of
SP-D within the bronchioles of infected lambs. Healthy weaned lambs were inoculated with either
pyrogen-free saline (controls) or M. haemolytica intrabronchially using a fiber-optic
bronchoscope.
SP-D protein and
mRNA expression in lung was detected by immunohistochemistry (IHC) and fluorogenic real-time relative quantitative
reverse transcriptase polymerase chain reaction (real-time RT-PCR), respectively, during acute (1 day), subacute (15 days), and chronic (45 days)
bronchopneumonia. At 15 and 45 days post-inoculation, areas of lung had peribronchiolar inflammatory cell infiltrate, epithelial cell
hyperplasia, tortuosity of the airway lumens, and decreased intensity of
SP-D protein staining and number of positive cells. The levels of
SP-D mRNA were not increased or significantly altered by M. haemolytica
infection when compared to control animals. In conclusion, cell-associated
SP-D protein expression significantly decreases within hyperplastic epithelium of lungs from infected animals during chronic
bronchopneumonia. Exhaustion of
SP-D protein reserves and absence of
SP-D gene upregulation during the progression of
bacterial pneumonia into chronicity may result in failure to clear the pathogen from the lung and/or cause animals to be more susceptible to
re-infection.