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7 results on '"Adnan, Muhammad"'

1. Improving boron use efficiency via different application techniques for optimum production of good quality potato (Solanum tuberosum L.) in alkaline soil

Author

Tariq, Muhammad, primary, Ahmad, Bilal, additional, Adnan, Muhammad, additional, Mian, Ishaq Ahmad, additional, Khan, Shadman, additional, Fahad, Shah, additional, Saleem, Muhammad Hamzah, additional, Ali, Mukhtiar, additional, Mussarat, Maria, additional, Ahmad, Manzoor, additional, Romman, Muhammad, additional, Chattha, Muhammad Sohaib, additional, El-Sheikh, Mohamed A., additional, and Ali, Shafaqat, additional

Published
2022
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2. The impact of aqueous and N-hexane extracts of three Fabaceae species on seed germination and seedling growth of some broadleaved weed species

Author

Safdar, Muhammad Ehsan, primary, Wang, Xiukang, additional, Abbas, Mudasar, additional, Ozaslan, Cumali, additional, Asif, Muhammad, additional, Adnan, Muhammad, additional, Zuan, Ali Tan Kee, additional, Wang, Wenqiang, additional, Gasparovic, Kristina, additional, Nasif, Omaima, additional, and Ansari, Mohammad Javed, additional

Published
2021
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4. Human L-ficolin, a recognition molecule of the lectin activation pathway of complement, activates complement by binding to pneumolysin, the major toxin of Streptococcus pneumoniae.

Author

Youssif M Ali, Hany I Kenawy, Adnan Muhammad, Robert B Sim, Peter W Andrew, and Wilhelm J Schwaeble

Subjects
Medicine, Science
Abstract

The complement system is an essential component of the immune response, providing a critical line of defense against different pathogens including S. pneumoniae. Complement is activated via three distinct pathways: the classical (CP), the alternative (AP) and the lectin pathway (LP). The role of Pneumolysin (PLY), a bacterial toxin released by S. pneumoniae, in triggering complement activation has been studied in vitro. Our results demonstrate that in both human and mouse sera complement was activated via the CP, initiated by direct binding of even non-specific IgM and IgG3 to PLY. Absence of CP activity in C1q(-/-) mouse serum completely abolished any C3 deposition. However, C1q depleted human serum strongly opsonized PLY through abundant deposition of C3 activation products, indicating that the LP may have a vital role in activating the human complement system on PLY. We identified that human L-ficolin is the critical LP recognition molecule that drives LP activation on PLY, while all of the murine LP recognition components fail to bind and activate complement on PLY. This work elucidates the detailed interactions between PLY and complement and shows for the first time a specific role of the LP in PLY-mediated complement activation in human serum.

Published
2013
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7. Human L-ficolin, a recognition molecule of the lectin activation pathway of complement, activates complement by binding to pneumolysin, the major toxin of Streptococcus pneumoniae

Author

Adnan Muhammad, Peter W. Andrew, Youssif M. Ali, Wilhelm J. Schwaeble, Robert B. Sim, and Hany I. Kenawy

Subjects
Adult, lcsh:Medicine, Complement receptor, Complement factor B, Microbiology, 03 medical and health sciences, 0302 clinical medicine, Bacterial Proteins, Lectins, Humans, lcsh:Science, Complement C1q, Complement Activation, 030304 developmental biology, 0303 health sciences, Multidisciplinary, biology, Complement component 2, lcsh:R, Complement Pathway, Mannose-Binding Lectin, Complement C3, Complement System Proteins, Recombinant Proteins, 3. Good health, Complement system, Cell biology, Lectin pathway, Factor H, Streptolysins, biology.protein, lcsh:Q, 030215 immunology, Complement control protein, Protein Binding, Research Article
Abstract

The complement system is an essential component of the immune response, providing a critical line of defense against different pathogens including S. pneumoniae. Complement is activated via three distinct pathways: the classical (CP), the alternative (AP) and the lectin pathway (LP). The role of Pneumolysin (PLY), a bacterial toxin released by S. pneumoniae, in triggering complement activation has been studied in vitro. Our results demonstrate that in both human and mouse sera complement was activated via the CP, initiated by direct binding of even non-specific IgM and IgG3 to PLY. Absence of CP activity in C1q(-/-) mouse serum completely abolished any C3 deposition. However, C1q depleted human serum strongly opsonized PLY through abundant deposition of C3 activation products, indicating that the LP may have a vital role in activating the human complement system on PLY. We identified that human L-ficolin is the critical LP recognition molecule that drives LP activation on PLY, while all of the murine LP recognition components fail to bind and activate complement on PLY. This work elucidates the detailed interactions between PLY and complement and shows for the first time a specific role of the LP in PLY-mediated complement activation in human serum.

Published
2013

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