Publications by authors named "Nur Shidaa Mohd Ali"

causes motile septicemia (MAS), a disease with a high mortality rate in tilapia culture. Feed-based vaccines with the incorporation of inactivated whole-cell bacteria into the feed offer promising tools to control MAS. Currently, the incorporation of genome-free bacteria as bacterial vaccine through the implementation of SimCells technology into the feed has become a particular interest.

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Feed-based bivalent vaccine (FBBV) containing killed whole organism (KWO) of Streptococcus agalactiae and Aeromonas hydrophila with 10% palm oil was previously proved to improve red hybrid tilapia's (Oreochromis sp.) immunity against streptococcosis and Aeromonas infections. This study characterized the FBBV's stability following the preparatory process and storage.

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Previous studies have proven that red hybrid tilapia ( sp.) vaccinated with a feed-based bivalent vaccine incorporating the formalin-killed whole organisms and mixed with 10 % palm oil showed good protection against streptococcosis and aeromoniasis diseases. However, the molecular mechanisms related to the induction of fish's immunological responses after vaccination are poorly investigated.

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Streptococcosis and aeromoniasis are the main obstacles to sustainable tilapia production. Vaccination offered an effective method to control microbial infections. Previously, a feed-based bivalent vaccine (FBBV) containing killed whole organisms of Streptococcus agalactiae and Aeromonas hydrophila mixed with 10% palm oil was successfully developed, which provided good protection against streptococcosis and aeromoniasis in Oreochromis sp.

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Streptococcosis and motile Aeromonad septicemia (MAS) are the main bacterial diseases in tilapia culture worldwide, causing significant economic losses. Vaccination is an effective method of preventing diseases and contributes to economic sustainability. This study investigated the immuno-protective efficacy of a newly developed feed-based bivalent vaccine against streptococcosis and MAS in red hybrid tilapia.

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Calcium-binding plays a decisive role in the folding and stabilization of many RTX proteins, especially for the RTX domain. Although many studies have been conducted to prove the contribution of Ca ion toward the folding and stabilization of RTX proteins, its functional dynamics and conformational structural changes remain elusive. Here, molecular docking and molecular dynamics (MD) simulations were performed to analyze the contribution of Ca ion toward the folding and stabilization of the RTX lipase (AMS8 lipase) structure.

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It is hypothesized that the Ca ions were involved in the activity, folding and stabilization of many protein structures. Many of these proteins contain repeat in toxin (RTX) motifs. AMS8 lipase from Antarctic strain AMS8 was found to have three RTX motifs.

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