Authorship Concerns and Who Truly Owns a Research Idea?

Researchers often face dilemmas about authorship. When the researchers are graduate students, fellows, or junior faculty, the dilemmas might involve discussions about fair criteria for more senior faculty to be acknowledged as key contributors or authors on manuscripts. This "Ethics Rounds" presents a case in which a fellow faced such a dilemma.

The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion.

In pathogenic Gram-negative bacteria, many virulence factors are secreted via the two-partner secretion pathway, which consists of an exoprotein called TpsA and a cognate outer membrane translocator called TpsB. The HMW1 and HMW2 adhesins are major virulence factors in nontypeable Haemophilus influenzae and are prototype two-partner secretion pathway exoproteins. A key step in the delivery of HMW1 and HMW2 to the bacterial surface involves targeting to the HMW1B and HMW2B outer membrane translocators by an N-terminal region called the secretion domain.

Evidence for conservation of architecture and physical properties of Omp85-like proteins throughout evolution.

Omp85-like proteins represent a family of proteins involved in protein translocation, and they are present in all domains of life, except archaea. In eukaryotes, Omp85-like proteins have been demonstrated to form tetrameric pore-forming complexes that interact directly with their substrate proteins. Studies performed with bacterial Omp85-like proteins have demonstrated pore-forming activity but no evidence of multimerization.

The Hemophilus influenzae Hap autotransporter is a chymotrypsin clan serine protease and undergoes autoproteolysis via an intermolecular mechanism.

The Hemophilus influenzae Hap adhesin is an autotransporter protein that undergoes an autoproteolytic cleavage event resulting in extracellular release of the adhesin domain (Hap(s)) from the membrane-associated translocator domain (Hap(beta)). Hap autoproteolysis is mediated by Ser(243) and occurs at LN1036-7 and to a lesser extent at more COOH-terminal alternate sites. In the present study, we sought to further define the mechanism of Hap autoproteolysis.

Molecular determinants of the interaction between Haemophilus influenzae and human cells.

Haemophilus influenzae is a human-specific pathogen that must colonize the human upper respiratory tract to avoid extinction. On occasion, organisms penetrate the epithelial barrier and cause bacteremic disease or spread within the respiratory tract to produce localized disease. Attachment to host epithelium is fundamental to the process of colonization and to the pathogenesis of disease.