Publications

PURPOSE

We evaluated a template for molecular genetic test reports that was developed as a strategy to reduce communication errors between the laboratory and ordering clinician.

METHODS

We surveyed 1,600 primary care physicians to assess satisfaction, ease of use, and effectiveness of genetic test reports developed using our template and reports developed by clinical laboratories. Mean score differences of responses between the reports were compared using t-tests. Two-way analysis of variance evaluated the effect of template versus standard reports and the influence of physician characteristics.

RESULTS

There were 396 (24%) respondents. Template reports had higher scores than the standard reports for each survey item. The gender and specialty of the physician did not influence scores; however, younger physicians gave higher scores regardless of report type. There was significant interaction between report type and whether physicians ordered or reviewed any genetic tests (none versus at least one) in the past year, P = 0.005.

CONCLUSION

For each survey item assessing satisfaction, ease of use, and effectiveness, physicians gave higher ratings to genetic test reports developed with the template than standard reports used by clinical laboratories. Physicians least familiar with genetic test reports, and possibly having the greatest need for better communication, were best served by the template reports.

The accessory Sec system of Streptococcus gordonii is comprised of SecY2, SecA2, and five proteins (Asp1 through -5) that are required for the export of a serine-rich glycoprotein, GspB. We have previously shown that a number of the Asps interact with GspB, SecA2, or each other. To further define the roles of these Asps in export, we examined their subcellular localization in S. gordonii and in Escherichia coli expressing the streptococcal accessory Sec system. In particular, we assessed how the locations of these accessory Sec proteins were altered by the presence of other components. Using fluorescence microscopy, we found in E. coli that SecA2 localized within multiple foci at the cell membrane, regardless of whether other accessory Sec proteins were expressed. Asp2 alone localized to the cell poles but formed a similar punctate pattern at the membrane when SecA2 was present. Asp1 and Asp3 localized diffusely in the cytosol when expressed alone or with SecA2. However, these proteins redistributed to the membrane in a punctate arrangement when all of the accessory Sec components were present. Cell fractionation studies with S. gordonii further corroborated these microscopy results. Collectively, these findings indicate that Asp1 to -3 are not integral membrane proteins that form structural parts of the translocation channel. Instead, SecA2 serves as a docking site for Asp2, which in turn attracts a complex of Asp1 and Asp3 to the membrane. These protein interactions may be important for the trafficking of GspB to the cell membrane and its subsequent translocation.