TY - JOUR
T1 - Synthesis of aspartic acid and tyrosine by the fire blight pathogen Erwinia amylovora is not required for proliferation on apple flower stigmas or virulence in fruitlets
AU - Schultes, Neil P.
AU - Sinn, Judith Pawloski
AU - Swenson, Eric S.
AU - McNellis, Timothy W.
N1 - Publisher Copyright:
© 2024 The Author(s).
PY - 2024/8
Y1 - 2024/8
N2 - Aims: The Gram-negative bacterium Erwinia amylovora (Ea) is the causal agent of fire blight, a devastating disease of apples and pears. In the fire blight disease cycle, Ea grows in different plant tissues, each presenting a distinct nutrient environment. Here, we investigate the ability of aspartate and tyrosine double auxotroph Ea lines to proliferate on apple flower stigma surfaces representing the epiphytic growth stage of Ea and in developing fruitlets representing one endophytic growth stage of Ea. Methods and results: Heterologous complementation studies in an Escherichia coli aspartate and tyrosine auxotroph verify that Ea aspartate aminotransferase (AspC) and tyrosine aminotransferase (TyrB) act as aspartate and tyrosine amino transferases. Growth analysis reveals that Ea aspC tyrB mutants multiply to near-wild-type levels on apple flower stigmas and immature fruitlets. Conclusions: Ea AspC and TyrB are reciprocally complementing for aspartate and tyrosine synthesis in Ec and in Ea. Ea aspC and tyrB mutants obtain sufficient aspartate and tyrosine to support multiplication on stigma surfaces and virulence in immature fruitlets.
AB - Aims: The Gram-negative bacterium Erwinia amylovora (Ea) is the causal agent of fire blight, a devastating disease of apples and pears. In the fire blight disease cycle, Ea grows in different plant tissues, each presenting a distinct nutrient environment. Here, we investigate the ability of aspartate and tyrosine double auxotroph Ea lines to proliferate on apple flower stigma surfaces representing the epiphytic growth stage of Ea and in developing fruitlets representing one endophytic growth stage of Ea. Methods and results: Heterologous complementation studies in an Escherichia coli aspartate and tyrosine auxotroph verify that Ea aspartate aminotransferase (AspC) and tyrosine aminotransferase (TyrB) act as aspartate and tyrosine amino transferases. Growth analysis reveals that Ea aspC tyrB mutants multiply to near-wild-type levels on apple flower stigmas and immature fruitlets. Conclusions: Ea AspC and TyrB are reciprocally complementing for aspartate and tyrosine synthesis in Ec and in Ea. Ea aspC and tyrB mutants obtain sufficient aspartate and tyrosine to support multiplication on stigma surfaces and virulence in immature fruitlets.
UR - http://www.scopus.com/inward/record.url?scp=85200769349&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85200769349&partnerID=8YFLogxK
U2 - 10.1093/jambio/lxae185
DO - 10.1093/jambio/lxae185
M3 - Article
C2 - 39085039
AN - SCOPUS:85200769349
SN - 1364-5072
VL - 135
JO - Journal of Applied Microbiology
JF - Journal of Applied Microbiology
IS - 8
M1 - lxae185
ER -