Bacteriol . Joseph W . St . Geme III and David Cutter Associated Uncleaved at the C Terminus and Fully Cell an Autotransporter Protein That Remains Hia Adhesin Is
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Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter.
Haemophilus influenzae is an important human pathogen that initiates infection by colonizing the upper respiratory tract. The H. influenzae Hia autotransporter is an adhesive protein that promotes adherence to respiratory epithelial cells. Hia adhesive activity resides in two homologous binding domains, called HiaBD1 and HiaBD2. These domains interact with the same host cell receptor, but bind ...
متن کاملImmunization with Haemophilus influenzae Hap adhesin protects against nasopharyngeal colonization in experimental mice.
Nontypeable Haemophilus influenzae is a common cause of respiratory tract disease and initiates infection by colonizing the nasopharynx. The H. influenzae Hap adhesin is an autotransporter protein that was discovered because it promotes intimate interaction with human epithelial cells. Hap contains an extracellular domain called Hap(s) that has adhesive and protease activity and an outer membra...
متن کاملStructure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter.
Autotransporter proteins are defined by the ability to drive their own secretion across the bacterial outer membrane. The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adhesion to the respiratory epithelium. In this report, we present the crystal structure of the C-terminal end of Hia, corresponding to the entire Hia trans...
متن کاملTrimeric autotransporters require trimerization of the passenger domain for stability and adhesive activity.
In recent years, structural studies have identified a number of bacterial, viral, and eukaryotic adhesive proteins that have a trimeric architecture. The prototype examples in bacteria are the Haemophilus influenzae Hia adhesin and the Yersinia enterocolitica YadA adhesin. Both Hia and YadA are members of the trimeric-autotransporter subfamily and are characterized by an internal passenger doma...
متن کاملThe C-terminal fragment of the internal 110-kilodalton passenger domain of the Hap protein of nontypeable Haemophilus influenzae is a potential vaccine candidate.
Nontypeable Haemophilus influenzae is a major causative agent of bacterial otitis media in children. H. influenzae Hap autotransporter protein is an adhesin composed of an outer membrane Hapbeta region and a moiety of an extracellular internal 110-kDa passenger domain called Hap(S). The Hap(S) moiety promotes adherence to human epithelial cells and extracellular matrix proteins, and it also med...
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