Preparation of Phytoplasma Membrane Recombinant Proteins

Galetto, Luciana; Siampour, Majid; Marzachı̀, Cristina

doi:10.1007/978-1-62703-089-2_30

Search citation statements

Order By: Relevance

Paper Sections

Select...

Protein Isolation and Recombinant Expression1

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2016

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

(1 citation statement)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Taken together, these studies demonstrate that IDPs can be expressed in E. coli and purified via histidine fusion tagging (for a detailed protocol see Galetto et al, 2013).…”

Section: Protein Isolation and Recombinant Expressionsupporting

confidence: 41%

Immunodominant membrane proteins of phytoplasmas

2016

View full text Add to dashboard Cite

Phytoplasmas are plant-pathogenic, phloem-colonizing, cell wall-less microorganisms that are primarily dependent on insect transmission for their spread and survival. The life cycle of phytoplasmas involves replication in insects and host plants. Until recently, phytoplasmas have resisted all attempts at cultivation in cell-free media, making these pathogens poorly characterized on a physiological and biochemical basis. However, host-pathogen relationships can be studied by investigating immunodominant membrane proteins (IDPs), which are located on the exterior surfaces of phytoplasma cells and are the most abundant proteins of the cell membrane. These membrane proteins come in direct contact with both insect and plant hosts and are thought to play a crucial role in phytoplasma spread both within the plant and by insect vectors. Therefore, there is great interest in studying this class of proteins. We summarize and discuss important investigations about these membrane proteins, which have already provided a better understanding of the host-phytoplasma relationship.

show abstract

“…Taken together, these studies demonstrate that IDPs can be expressed in E. coli and purified via histidine fusion tagging (for a detailed protocol see Galetto et al, 2013).…”

Section: Protein Isolation and Recombinant Expressionsupporting

confidence: 41%