Journal Issue: JAAS Vol. 7 No. 1
3
Issued Date
2557
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Language
tha
eng
eng
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application/pdf
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open access
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ผลงานนี้เป็นลิขสิทธิ์ของมหาวิทยาลัยมหิดล ขอสงวนไว้สำหรับเพื่อการศึกษาเท่านั้น ต้องอ้างอิงแหล่งที่มา ห้ามดัดแปลงเนื้อหา และห้ามนำไปใช้เพื่อการค้า
Rights Holder(s)
คณะสัตวแพทยศาสตร์ มหาวิทยาลัยมหิดล
Journal Volume
JAAS Volume 7
(2557)
Articles
Subtilisin-like proprotein convertases (SPCs); host enzymes controlled viral protein processing and maturation
(2014) Kridsada Chaichoun; Mahidol University. Faculty of Veterinary Science. Department of Pre-clinic and Applied Animal Science
The cellular subtilisin-like proprotein convertases (SPCs) are responsible for virion maturation process
which occurs in secretory vesicles, primes virion maturation and viral infectivity. Eight SPCs, SPC1 (furin/PACE),
SPC2 (PC2), SPC3 (PC1/PC3), SPC4 (PACE4), SPC5 (PC4), SPC6 (PC5/PC6A) and SPC7 (LPC/PC7/PC8)
and PCSK9, were identified. The consensus substrate sequence is -RX(K/R)R▼X- (X can be any amino acid, ▼
represents the cleavage site). The conformational change of viral proteins can be triggered by a low pH in the
endosomes, as in the case of influenza virus, or by the interaction with a secondary receptor protein at the cell
surface, as the case of HIV. In flaviviruses, the functional roles of charged residues locate to the SPC consensus
sequence in cleavage site of prM protein and provide cleavability affect to virus replication. Changes in the
prM-cleavage level were associated with altered proportions of extracellular virions and subviral particles.
The hemagglutinin (HA) protein is a critical determinant of the pathogenicity of avian influenza viruses, with a
clear link between HA cleavability and virulence. The highly pathogenic avian influenza virus, in which
contain high numbers of basic amino acid sequence at the HA cleavage site, can be converted to low numbers
of basic amino acid sequence of a typical avirulent virus. The processing by SPCs is an important control
mechanism for the biological activity of viral surface proteins. The molecular mechanisms underlying the
recognition of SPCs by viral glycoproteins were described, including recent findings demonstrating differential
SPC-recognition of viral and cellular substrates. Proteolytic activation of envelope glycoproteins is necessary for
entry of viruses into the host cell and, hence, for their ability to undergo multiple replication cycles. Proteolytic
cleavage is the first step in the activation of virus fusion proteins and is followed by a conformational change
resulting in the exposure of the fusion domain. The conformational change can be triggered by a low pH in the
endosomes, or by the interaction with a secondary receptor protein at the cell surface.
ความชุกทางซีรั่มของการติดเชื้อบรูเซลลาในโคเนื้อ อำเภอไทรโยค จังหวัดกาญจนบุรี
(2557) วิษณุ วงษ์สว่าง; สุวรรณา แสนยุติธรรม; เชาวลิต นาคทอง; มหาวิทยาลัยมหิดล. คณะสัตวแพทยศาสตร์
The objective of this study is a seroprevalence of Brucella spp. infection in beef cattle in Sai-Yok
district, Karnchanaburi province. The serological methods were carried out using Rose Bengal Test (RBT)
and indirect Enzyme-Linked Immunosorbent Assay (indirect-ELISA) in 300 beef. Results showed that 4.33%
in individual prevalence for brucellosis, 30.43% in farms prevalence, 4.7% in a male beef, 4.18% in a
female beef, and a male beef is more probable than a female beef (OR = 1.130, 95% CI = 0.339-3.774,
P-value = 0.842). In addition, the prevalence was found that 5.21% in older three years old beef group, 1.42%
in younger three years old beef group. Moreover, an older beef (> 3 years old beef group) is brucellosis
more probable than a young beef (< 3 years old beef group) (OR = 3.798, 95% CI = 0.485 - 29.737, P-value = 0.204).
การสำรวจความชุกพยาธิภายในทางเดินอาหารของโคเนื้อ อำเภอไทรโยค จังหวัดกาญจนบุรี
(2557) วิษณุ วงษ์สว่าง; สุวรรณา แสนยุติธรรม; เชาวลิต นาคทอง; มหาวิทยาลัยมหิดล. คณะสัตวแพทยศาสตร์
Between March 2010 and February 2012, fecal samples from 309 beef cattle at Sai-Yok district,
Kanchanaburi, Thailand were used to determine the prevalence of gastro-intestinal (GI) parasites infection and
to examine the associated determinants i.e. sex, age, and management. The overall prevalence of GI parasites
was 86.4% (267/309). The important parasites identified were Strongylids 71.84% (222/309), followed by
rumen fluke 20.06% (65/309) and Strongyloides papillosus 17.15% (53/309). The protozoan infection of coccidian
oocysts (5.5% 17/309) was also observed. Female cattle, cattle older than 3 years, and native cattle showed the
higher prevalent rate including those feed in the grazing pasture. This result provides a basal line data of
GI parasites infection which can be used for treatment and control strategies against GI parasites in the future.
การสำรวจแมลงวันคอกสัตว์ Stomoxys spp. (Diptera: Muscidae) บริเวณคอกม้า คณะสัตวแพทยศาสตร์ มหาวิทยาลัยมหิดล จังหวัดนครปฐม
(2557) ธนาวลี หมั่นเทียนติพันธ์; นุชนารถ ใช้บางยาง; ทิฆเวท เวฬุวนารักษ์; ปุญญพัฒน์ เศษวิสัย; ธนศักดิ์ ช่างบรรจง; มหาวิทยาลัยมหิดล. คณะสัตวแพทยศาสตร์
Stable flies are important blood sucking flies of livestock and other mammals. They can transmit many
parasites and pathogens. The present study was carried out to survey the stable flies at the horse stable of
Faculty of Veterinary Science, Mahidol University from July to August 2013 using Vavoua traps. A total of
976 individuals of 2 species were captured; Stomoxys calcitrans (97.75%) and Stomoxys indicus (2.25%).
The diurnal feeding activity of each species was observed during different period of times (06.00 to 18.00).
Males of S. calcitrans showed peak of diurnal activity in the morning (08.00 to 10.00) and in the afternoon
(14.00 to 16.00) whereas females showed a constant activity throughout the day. Both sexes of S. indicus
showed peak of activity in the early morning (06.00 to 08.00) and the late afternoon (16.00 to 18.00). Some
morphological characters (frontal index and body length) in both sexes of each species were also measured.
Results of this study provide information that may be useful for stable fly control programs.
Title
JAAS Vol. 7 No. 1
Author's Affiliation
มหาวิทยาลัยมหิดล. คณะสัตวแพทยศาสตร์