User:Cedombroski/sandbox

Practice
This is my sandbox page. I am currently learning to use wiki markup.

This is bold formatting.

Article Evaluation

 * Everything is relevant to the topic, however the organization of the major and minor diseases could do with different formatting.
 * The article is neutral.
 * The links available work, but there are some paragraphs with claims that do not have any citations.
 * The talk page gives suggestions as to how to improve the organization and content of the article, as well as suggestions of other topics to add.

Article Selection

 * Articles: Merozoite surface protein, Growth-hormone-releasing hormone receptor, Anti-Müllerian hormone receptor, Aneugen
 * Content in each article is relevant, however there is very minimal information, and each article can definitely be expanded to include updated research related to the topic.
 * All articles are written neutrally.
 * The Merozoite Surface Protein and Anti-Müllerian hormone receptor articles have very few citations and could do with many more.
 * Citations appear reliable.

-These all seems like viable options. CHoose the one that interests you most. Be mindful of not getting repetitive on the AMH receptor page with information about AMH itself. - Dr. Tienson-Tseng

Forms and Function
The most common form of MSPs are anchored to the merozoite surface with glycophosphatidylinositol, a short glycolipid often used for protein anchoring. Additional forms include integral membrane proteins and peripherally associated proteins, which are found to a lesser extent than glycophosphatidylinositol anchored proteins, or (GPI)-anchored proteins, on the merozoite surface. Merozoite surface proteins 1 and 2 are the most abundant (GPI)-anchored proteins on the surface of Plasmodium merozoites. MSP-1 is synthesized at the very beginning of schizogony, or asexual merozoite reproduction. The merozoite first attaches to a red blood cell using its MSP-1 complex. The MSP-1 complex targets spectrin, a complex on the internal surface of the cell membrane of a red blood cell. The majority of the MSP-1 complex is shed upon entry into the red blood cell, but a small portion of the C-terminus, called MSP-119, is conserved. The exact role of MSP-119 remains unknown, but it serves as a marker for the formation of the food vacuole. The function of the MSP-2 complex is not concrete, but current research suggests it has a role in red blood cell invasion due to its degradation shortly after invasion. MSP- 3, 6, 7 and 9 are peripheral membrane proteins that have been shown to form a complex with MSP-1, but the functions of these proteins are largely unknown.

Clinical Significance
Due to their prevalence on the Plasmodium surface, MSPs have been a key target for vaccine development. Anti-malarial vaccines have been developed to target the merozoite at different stages in its life cycle. Vaccines that target the merozoite in its asexual erythrocytic stage utilize merozoite surface proteins, particularly MSP-1. The biggest challenge faced when developing these vaccines is the high complexity and variation of these proteins. In merozoites of the same genus and species, the sequences encoding proteins such as MSP-1 vary greatly depending on the region they are found. For example, the Combination B vaccine utilizes antigens of MSP-1 and MSP-2 but has limited efficacy based primarily on the MSP-2 alleles used. In an attempt to increase the efficiency of vaccines produced, constant regions such as MSP-119 which remain on the surface of the Plasmodium after the merozoite stage are becoming a key focus for vaccine studies. Additionally, synthetic glycophosphatidylinositol (GPI) molecules are emerging as a potential candidate due to their ability to elicit a strong immune response while simultaneously remaining relatively consistent in structure throughout various malarial strains.

In addition to vaccines, researchers are developing drugs that bind to MSPs in order to disrupt merozoite replication. Suramin, a drug used to treat African sleeping sickness, has shown moderate success with binding to MSP-1 and its derivatives such as MSP-119 to inhibit red blood cell invasion.