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Rapid Identification of Phospholipase A₂ Transcripts from Snake Venoms.

ABSTRACT: Phospholipase A₂ (PLA₂) is a major component in snake venoms and it is found in many different isoforms. To identify transcripts encoding different PLA₂ isoforms, we developed a simple, rapid procedure. Total RNA was extracted from the venoms of three cottonmouth snakes and two diamondback rattlesnakes, and further reverse-transcribed into complementary DNA (cDNA). Using one pair of cottonmouth PLA₂-specific primers and a Reverse Transcription Polymerase Chain Reaction (RT-PCR) technique, we identified 27 unique full-length PLA₂ transcripts, including nine sequences identical to the previously documented ones in the database and one novel GIII-like PLA₂. Two common transcripts respectively encoding Asp49 and Lys49 PLA₂ isoforms were identified in all three cottonmouth venoms, that contain more PLA₂ transcripts than the diamondback rattlesnake venoms. The placement of cloned PLA₂ transcripts in snake venom PLA₂s was further discussed by phylogenetic analysis. The procedure developed in this study paves the way for accelerated acquisition of transcriptome data on any other venom toxin families. The results obtained are crucial for insight into the structure and function of PLA₂ isoforms for scientific and potential therapeutic purposes.

SUBMITTER: Jia Y

PROVIDER: S-EPMC6409593 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Protozoal infection is a lingering public health issue of great concern, despite efforts to produce drugs and vaccines against it. Recent breakthrough research has discovered alternative antiprotozoal agents encompassing the use of snake venoms and their components to cure these infections. This study collated the existing literature to examine the antiprotozoal effect of snake venoms and their fractions. We conducted a systematic review following the PRISMA guidelines. The PubMed and Embase databases were searched from their inception until 13 October 2021. Articles were screened at the title, abstract and full-text phases. Some additional studies were obtained through the manual search process. We identified 331 studies via the electronic database and manual searches, of which 55 reporting the antiprotozoal effect of snake venoms and their components were included in the review. Around 38% of studies examined the effect of whole crude venoms, and a similar percentage evaluated the effect of a proportion of enzymatic phospholipase A2 (PLA2). In particular, this review reports around 36 PLA2 activities and 29 snake crude venom activities. We also report the notable phenomenon of synergism with PLA2 isoforms of Bothrops asper. Importantly, limited attention has been given so far to the antiprotozoal efficacies of metalloproteinase, serine protease and three-finger toxins, although these venom components have been identified as significant components of the dominant venom families. This study highlights the impact of snake venoms and their fractions on controlling protozoal infections and suggests the need to examine further the effectiveness of other venom components, such as metalloproteinase, serine protease and three-finger toxins. Future research questions in this field must be redirected toward synergism in snake venom components, based on pharmacological usage and in the context of toxicology. Ascertaining the effects of snake venoms and their components on other protozoal species that have not yet been studied is imperative.

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Rapid Identification of Phospholipase A₂ Transcripts from Snake Venoms.

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