A fine - tuned interaction between the trimeric autotransporter 1 Haemophilus surface fibrils and vitronectin leads to serum resistance 2 and adherence to respiratory epithelial cells

نویسندگان

  • Birendra Singh
  • Yu-Ching Su
  • Tamim Al-Jubair
  • Oindrilla Mukherjee
  • Teresia Hallström
  • Matthias Mörgelin
  • Anna M. Blom
  • Kristian Riesbeck
چکیده

Medical Microbiology, Department of Laboratory Medicine Malmö, Lund University, Jan 7 Waldenströms gata 59, SE-205 02 Malmö, Sweden, Department of Infection Biology, Leibniz 8 Institute for Natural Product Research and Infection Biology, Hans-Knoell-Institute, D-07745 9 Germany, Section of Clinical and Experimental Infectious Medicine, Department of Clinical 10 Sciences, Lund University, SE-221 84 Lund, Sweden, and Division of Medical Protein Chemistry, 11 The Wallenberg Laboratory, Department of Laboratory Medicine Malmö, Lund University, 12 Skåne University Hospital, SE-205 02 Malmö, Sweden. 13

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

A fine-tuned interaction between trimeric autotransporter haemophilus surface fibrils and vitronectin leads to serum resistance and adherence to respiratory epithelial cells.

Haemophilus influenzae type b (Hib) escapes the host immune system by recruitment of the complement regulator vitronectin, which inhibits the formation of the membrane attack complex (MAC) by inhibiting C5b-C7 complex formation and C9 polymerization. We reported previously that Hib acquires vitronectin at the surface by using Haemophilus surface fibrils (Hsf). Here we studied in detail the inte...

متن کامل

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 کامل

A BCAM0223 Mutant of Burkholderia cenocepacia Is Deficient in Hemagglutination, Serum Resistance, Adhesion to Epithelial Cells and Virulence

Burkholderia cepacia complex (Bcc) bacteria are a problematic group of microorganisms causing severe infections in patients with Cystic Fibrosis. In early stages of infection, Bcc bacteria must be able to adhere to and colonize the respiratory epithelium. Although this is not fully understood, this primary stage of infection is believed to be in part mediated by a specific type of adhesins, nam...

متن کامل

Chromosomal expression of the Haemophilus influenzae Hap autotransporter allows fine-tuned regulation of adhesive potential via inhibition of intermolecular autoproteolysis.

The Haemophilus influenzae Hap autotransporter is a nonpilus adhesin that promotes adherence to respiratory epithelial cells and selected extracellular matrix proteins and facilitates bacterial aggregation and microcolony formation. Hap consists of a 45-kDa outer membrane translocator domain called Hap(beta) and a 110-kDa extracellular passenger domain called Hap(S). All adhesive activity resid...

متن کامل

Haemophilus influenzae surface fibril (Hsf) is a unique twisted hairpin-like trimeric autotransporter.

The Haemophilus surface fibril (Hsf) is an extraordinary large (2413 amino acids) trimeric autotransporter, present in all encapsulated Haemophilus influenzae. It contributes to virulence by directly functioning as an adhesin. Furthermore, Hsf recruits the host factor vitronectin thereby inhibiting the host innate immune response resulting in enhanced survival in serum. Here we observed by elec...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2014