The study aims to explore the problems of the existing Shariah Governance Framework (SGF) and its concerned authorities in the context of Bangladesh. Thus, according to responses from 17 respondents, this study outlines that Bangladesh has an absence of a shortage of experts, experienced, knowledgeable, and qualified Shariah people at all levels (i.e., the central bank, Islamic banks, Shariah Supervisory Boards (SSBs), and regulators). Therefore, Bangladesh does not have a separate Islamic banking act, Shariah audit firm, Shariah index institutions, and comprehensive SGF. The existing guideline has a limitation concerning its comprehensiveness, accountability, responsibility, and structure of SSBs. Islamic banks do not follow the instruction of the central bank in the formation of SSBs. As a result, there is an absence of competent and qualified SSB, which also results in the functions of Shariah departments as well as Shariah applications. Usually, the Board of Directors (BOD), management, executives, customers, and the public also have the conceptual gap about Islamic banks, SGF, and banking system compared to the regular prayers, faith, and belief. Concisely, Bangladesh requisites a comprehensive SGF, Islamic banking act, a standard accounting system, and a robust Shariah audit system for the overall development of Islamic banks and SGF.

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Purpose: Construction of antibody-based, molecular-targeted optical imaging probes requires the labeling of an antibody with a fluorophore. The most common method for doing this involves non-specifically conjugating a fluorophore to an antibody, resulting in poorly defined, heterogeneous imaging probes that often have suboptimal in vivo behavior. We tested a new strategy to site-specific label antibody-based imaging probes using the SpyCatcher/SpyTag protein ligase system. Procedures: We used the SpyCatcher/SpyTag protein ligase system to site specifically label nimotuzumab, an anti-EGFR antibody and an anti-HER3 diabody. To prevent the labeling from interfering with antigen binding, we introduced the SpyTag and SpyCatcher at the C-terminus of the antibody and diabody, respectively. Expression and binding properties of the C-terminal antibody-SpyTag and diabody-SpyCatcher fusions were similar to the antibody and diabody, indicating that the SpyTag and SpyCatcher fusions were well tolerated at this position. Sitespecific labeling of the antibody and diabody was performed in two steps. First, we labeled the SpyCatcher with IRDye800CW-Maleimide and the SpyTag with IRDye800CW-NHS. Second, we conjugated the IRDye800CW-SpyCatcher and the IRDye800CW-SpyTag to the antibody or diabody, respectively. We confirmed the affinity and specificity of the IRDye800CW-labeled imaging probes using biolayer interferometry and flow cytometry. We analyzed the in vivo biodistribution and tumor accumulation of the IRDye800CW-labeled nimotuzumab and anti-HER3 diabody in nude mice bearing xenografts that express EGFR and HER3, respectively. Results: Expression and binding properties of the C-terminal antibody-SpyTag and diabodySpyCatcher fusions were similar to the antibody and diabody, indicating that the SpyTag and SpyCatcher fusions were well tolerated at this position. We confirmed the affinity and specificity of the IRDye800CW-labeled imaging probes using biolayer interferometry and flow cytometry. We analyzed the in vivo biodistribution and tumor accumulation of the IRDye800CW-labeled nimotuzumab and anti-HER3 diabody in nude mice bearing xenografts that express EGFR and HER3, respectively. Site-specifically IRDye800CW-labeled imaging probes bound to their Md. Kausar Alam and Ayman El-Sayed contributed equally to this work. Electronic supplementary material The online version of this article (https:// doi.org/10.1007/s11307-018-1222-y) contains supplementary material, which is available to authorized users.Correspondence to: Humphrey Fonge; e-mail: humphrey.fonge@usask.ca, C. Geyer; e-mail: ron.geyer@usask.ca * The Author(s), 2018 immobilized targets, cells expressing these targets, and selectively accumulated in xenografts. Conclusions: These results highlight the ease and utility of using the modular SpyTag/ SpyCatcher protein ligase system for site-specific fluorescent labeling of protein-based imaging probes. Imaging probes labeled in this manner will be useful for optical imaging applications such as image-guided surger...

Exploiting the innate modularity of proteins has allowed advances across the fields of synthetic biology and biotechnology. By using standardized protein components as building blocks, complex, multiprotein assemblies with sophisticated functions can be generated; feats previously not possible with strictly genetic‐engineering approaches. The development of strategies for protein assembly is accelerating, pushing the boundaries of protein architecture. SpyTag and SpyCatcher protein ligase is a recent advance in this field that allows plug‐and‐play modularity by harnessing post‐translational protein assembly. Herein, we review the latest applications of this powerful tool including novel enzyme assemblies, modularizing protein display, and the generation of antibody and antibody‐like “devices” by using SpyTag/SpyCatcher technology.

Streptococcus mutans and Streptococcus sobrinus are the main causative agents of human dental caries. Current strategies for treating caries are costly and do not completely eradicate them completely. Passive immunization using nonhuman antibodies against Streptococcal surface antigens has shown success in human trials, however they often invoke immune reactions. We used phage display to generate human antigen-binding fragments (Fabs) against S. mutans and S. sobrinus. These Fabs were readily expressed in E. coli and bound to the surface S. mutans and S. sobrinus. Fabs inhibited sucrose-induced S. mutans and S. sobrinus biofilm formation in vitro and a combination of S. mutans and S. sobrinus Fabs prevented dental caries formation in a rat caries model. These results demonstrated that S. mutans and S. sobrinus Fabs could be used in passive immunization strategies to prevent dental caries. In the future, this strategy may be applied towards a caries therapy, whereby Fabs are topically applied to the tooth surface.