Proteomic Analysis of Vibrio parahaemolyticus-Stimulated Pinctada martensii Proteins for Antimicrobial Activity, Potential Mechanisms, and Key Components

<b>Background:</b> Bacterial infections are a major challenge in food processing and public health, and there is an urgent need to develop novel antimicrobial agents. <b>Objectives:</b> The purpose of this study is to investigate the potential mechanism and key components of <i>Pinctada martensii</i> antimicrobial proteins (Pm-Aps) to provide a theoretical basis for the development of novel antimicrobial agents. <b>Methods:</b> The researchers used <i>Vibrio parahaemolyticus</i> (VP) to stimulate <i>Pinctada martensii</i>, extracted the antimicrobial proteins, and analyzed their antimicrobial activities, potential mechanisms of action, and key components using proteomics. <b>Results:</b> The results showed that the antimicrobial activity of Pm-Aps, with broad-spectrum antimicrobial effects, was significantly enhanced after VP stimulation. This was associated with the upregulation of <i>LAAO</i>, <i>CHDH</i>, <i>TLR2</i>, <i>ATG16L1</i>, <i>BAK</i>, <i>CLCA4</i>, and <i>CASP8</i> and the downregulation of <i>MCM3</i>, <i>MCM5</i>, <i>DTYMK</i>, <i>PLK1</i>, <i>FBXO6</i>, <i>LPCAT3</i>, <i>GST</i>, <i>LAMTOR5</i>, <i>CYP17A</i>, <i>CTSA</i>, and <i>RRM1</i>. It is hypothesized that these proteins may inhibit bacterial growth and multiplication by activating immune-related signaling pathways, inhibiting DNA replication and repair, and inducing apoptosis and autophagy. Furthermore, it was found that <i>LAAO</i> may be a key component of the antimicrobial action of Pm-Aps, killing bacteria by catalyzing the oxidation of amino acids to produce hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>). <b>Conclusions:</b> These results strongly suggest that Pm-Aps is an effective antimicrobial protein, and it is expected that new <i>LAAO</i> can be obtained from Pm-Aps.

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Journal
Antibiotics
Published
2024-11-19
DOI
https://doi.org/10.3390/antibiotics13111100
Primary Topic
Antimicrobial Peptides and Activities
Type
article
Field-Weighted Citation Impact
0.00

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article

Proteomic Analysis of Vibrio parahaemolyticus-Stimulated Pinctada martensii Proteins for Antimicrobial Activity, Potential Mechanisms, and Key Components

Beiping Luo, Zhongqin Chen, Jialong Gao, Weiqiang Shen et al.
Antibiotics
Antimicrobial Peptides and Activities
article

Proteomic Analysis of Vibrio parahaemolyticus-Stimulated Pinctada martensii Proteins for Antimicrobial Activity, Potential Mechanisms, and Key Components

Beiping Luo, Zhongqin Chen, Jialong Gao, Weiqiang Shen, Bingbing Song, Haisheng Lin, Xiaoming Qin, Huina Zheng, Wenhong Cao
article en

Abstract

<b>Background:</b> Bacterial infections are a major challenge in food processing and public health, and there is an urgent need to develop novel antimicrobial agents. <b>Objectives:</b> The purpose of this study is to investigate the potential mechanism and key components of <i>Pinctada martensii</i> antimicrobial proteins (Pm-Aps) to provide a theoretical basis for the development of novel antimicrobial agents. <b>Methods:</b> The researchers used <i>Vibrio parahaemolyticus</i> (VP) to stimulate <i>Pinctada martensii</i>, extracted the antimicrobial proteins, and analyzed their antimicrobial activities, potential mechanisms of action, and key components using proteomics. <b>Results:</b> The results showed that the antimicrobial activity of Pm-Aps, with broad-spectrum antimicrobial effects, was significantly enhanced after VP stimulation. This was associated with the upregulation of <i>LAAO</i>, <i>CHDH</i>, <i>TLR2</i>, <i>ATG16L1</i>, <i>BAK</i>, <i>CLCA4</i>, and <i>CASP8</i> and the downregulation of <i>MCM3</i>, <i>MCM5</i>, <i>DTYMK</i>, <i>PLK1</i>, <i>FBXO6</i>, <i>LPCAT3</i>, <i>GST</i>, <i>LAMTOR5</i>, <i>CYP17A</i>, <i>CTSA</i>, and <i>RRM1</i>. It is hypothesized that these proteins may inhibit bacterial growth and multiplication by activating immune-related signaling pathways, inhibiting DNA replication and repair, and inducing apoptosis and autophagy. Furthermore, it was found that <i>LAAO</i> may be a key component of the antimicrobial action of Pm-Aps, killing bacteria by catalyzing the oxidation of amino acids to produce hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>). <b>Conclusions:</b> These results strongly suggest that Pm-Aps is an effective antimicrobial protein, and it is expected that new <i>LAAO</i> can be obtained from Pm-Aps.

AntibioticsVol. 13(11)
Guangdong Ocean University (CN)
Natural Science Foundation of Guangdong Province, Guangdong Ocean University, Modern Agricultural Technology Industry System of Shandong province
Openalex Percentile: Top 80%
Antimicrobial Peptides and Activities
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