최근 지구 환경의 변화와 무역의 자유화에 따라 해충의 유입 가능성이 높아지며 농·수출산업, 생태계파괴 등의 피해가 더욱 커질 것으로 예상된다. 이에 따라 검역현장에서의 신속한 해충의 동정 기술 개발의 중요성이 높아지고 있다. 본연구에서는 신속하고 간단한 고분자 물질의 질량분석방법인 MALDI-TOF (Matric Assisted Laser Desorption Ionization Time of Flight Mass Spectroscopy)를 이용하여 해충의 신속 정확한 동정방법을 개발하였다. 기존에 곤충의 유충 동정방법은 형태적 동정과 분자생물학적 방법으로 시간이 오래걸리거나 동정 단계가 복잡하다. 하지만 MALDI-TOF MS 의 동정방법은 다른 동정방법에 비해 15분 내외로 시간이 매우 절약되며, 개발된 프로토콜의 이용으로 편리함, 단순함 등에서 현장 활용성이 매우 높을 뿐만아니라 최근에 널리 활용되고 있는 DNA barcode 방법과 비교할 때 중요한 검역해충 및 유사종인 복숭아순나방, 복숭아순나방붙이, 복숭아심식나방에대한 종 판별 해상도가 유사한 수준으로 확인되어 현장 적용에 쉽게 적용이 가능한 새로운 기술로 사료된다.

A polydnavirus, Cotesia plutellae bracovirus (CpBV), is symbiotic to an endoparasitoid wasp, C.plutellae, which specifically parasitizes young larvae of the diamondback moth, Plutella xylostella. A recent study on CpBV replication by analysis of ovary transcriptome of C.Plutellae suggests several candidate coat protein genes. This study was conducted to confirm the coat protein genes by analyzing coat proteins of CpBV viral particles by a tandem mass MALDI-TOF. Immunoprecipitation of ovary protein extract with a polyclonal CpBV antibody captured three proteins named as p35, p60, and p70. More number of coat proteins were resolved in a protein extract directly from viral particles. All candidate coat proteins are analyzed in amino acid sequences by MALDI-TOF. A comprehensive analysis of viral proteomics and ovary transcriptome determined novel viral coat proteins from CpBV

Buckwheat is one of the traditional crops and has become a renewed target of interest or a popular crop as a healthy foodstuff, because it is a good source of cereal protein which is rich with essential amino acids. However, what is critical to our health is that buckwheat contains proteins which cause a allergy. Buckwheat allergy resulting from ingestion is caused by the storage proteins in the grain with molecular weights ranging from 15, 22, 35, 39 and 50 kDa proteins of the inner fractions to low, and there were clear differences in the protein compositions between the inner and outer buckwheat flour fractions. A major allergenic protein of buckwheat is Fag e 1 with molecular weight 22 kDa (BW22KD). Buckwheat allergy is an immunoglobulin E (IgE)-mediated hypersensitive response capable of causing anaphylactic shock. Buckwheat seeds were dissected to endosperm and embryo. From each fraction we extracted proteins and analyzed extracts by SDS-PAGE and 2-DE. On electrophoregrams of endosperm proteins, 6 intense bands were detected. The most intense corresponded to molecular weights ranging from 54 to 65 kDa. These proteins have been reported not to be allergenic. We show here that the allergenic buckwheat seed proteins are found only among embryo proteins. No allergenic proteins were found in the buckwheat endosperm. The results presented here lead to the proposal that patients with hypersensitivity to buckwheat flour should use only fine flour from buckwheat endosperm, as this fraction contains no allergenic proteins. At present, specific protein spots will be selected and in-gel digested for MALDI-TOF-TOF/MS analysis.